Metal-sulfur cluster biosynthetic enzyme [Posttranslational modification, protein turnover, chaperones];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312720   2 EEALKDSILGALEMVIDPELGIDIVNLGLVYKVNVDDEGVCTVDMTLTSMGCPMGPQIIDQVKTVLAEIPEIQDTEVNIV 81
Cdd:COG2151    5 AEPLEEEVWEALKTVYDPEIPVNIVDLGLIYDVEVDDDGRVKVTMTLTTPGCPAADVIPDDVEEALEEVPGVEDVEVELV 84

                         90
                 ....*....|....*...
gi 446312720  82 WSPPWTKDMMSRYAKIAL 99
Cdd:COG2151   85 WDPPWTPDRMSEEARLKL 102

Metal-sulfur cluster biosynthetic enzyme [Posttranslational modification, protein turnover, chaperones];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312720   2 EEALKDSILGALEMVIDPELGIDIVNLGLVYKVNVDDEGVCTVDMTLTSMGCPMGPQIIDQVKTVLAEIPEIQDTEVNIV 81
Cdd:COG2151    5 AEPLEEEVWEALKTVYDPEIPVNIVDLGLIYDVEVDDDGRVKVTMTLTTPGCPAADVIPDDVEEALEEVPGVEDVEVELV 84

                         90
                 ....*....|....*...
gi 446312720  82 WSPPWTKDMMSRYAKIAL 99
Cdd:COG2151   85 WDPPWTPDRMSEEARLKL 102

Iron-sulfur cluster assembly protein; This family has an alpha/beta topology, with 13 conserved hydrophobic residues at its core and a putative active site containing a highly conserved cysteine. Members of this family are involved in a range of physiological functions. The family includes PaaJ (PhaH) from Pseudomonas putida. PaaJ forms a complex with PaaG (PhaF), PaaI (PhaG) and PaaK (PhaI), which hydroxylates phenylacetic acid to 2-hydroxyphenylacetic acid. It also includes PaaD from Escherichia coli, a member of a multicomponent oxygenase involved in phenylacetyl-CoA hydroxylation. Furthermore, several members of this family are shown to be involved in iron-sulfur (FeS) cluster assembly. Iron-sulfur (FeS) clusters are inorganic co-factors that are are able to transfer electrons and act as catalysts. They are involved in diverse cellular processes including cellular respiration, DNA replication and repair, antibiotic resistance, and dinitrogen fixation. The biogenesis of such clusters from elemental iron and sulfur is an enzymatic process that requires a set of specialized proteins. Proteins containing this domain include the chloroplast protein HCF101 (high chlorophyll fluorescence 101), which has been described as an essential and specific factor for assembly of [4Fe-4S]-cluster-containing protein complexes such as the membrane complex Photosystem I (PSI) and the heterodimeric FTR (ferredoxin-thioredoxin reductase) complex and is involved in the assembly of [4Fe-4S] clusters and their transfer to apoproteins. The mature HCF101 protein contains this domain at the N-terminal as well as eight cysteine residues along the sequence. All cysteine residues are conserved among higher plants, but of the two cysteine residues located in this domain only Cys128 is highly conserved and is present in the highly conserved P-loop domain of the plant HCF101 (CKGGVGKS). SufT protein from Staphylococcus aureus is composed of this domain solely and is shown to be involved in the maturation of FeS proteins. Given all this data, it is hypothesized that this domain might play a role in FeS cluster assembly.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446312720    6 KDSILGALEMVIDPELGIDIVNLGLVYKVNVDDEGVcTVDMTLTSMGCPMGPQIIDQVKTVLAEIPEiQDTEVNI 80
Cdd:pfam01883   1 KAAVLAALRTVIDPETGVDLVSLGLVRNIDIEGGKV-SVDITLTYPACPAAEAIRADAEAALRALPG-EVVEVSV 73

Metal-sulfur cluster biosynthetic enzyme [Posttranslational modification, protein turnover, chaperones];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312720   2 EEALKDSILGALEMVIDPELGIDIVNLGLVYKVNVDDEGVCTVDMTLTSMGCPMGPQIIDQVKTVLAEIPEIQDTEVNIV 81
Cdd:COG2151    5 AEPLEEEVWEALKTVYDPEIPVNIVDLGLIYDVEVDDDGRVKVTMTLTTPGCPAADVIPDDVEEALEEVPGVEDVEVELV 84

                         90
                 ....*....|....*...
gi 446312720  82 WSPPWTKDMMSRYAKIAL 99
Cdd:COG2151   85 WDPPWTPDRMSEEARLKL 102

probable FeS assembly SUF system protein SufT; The function is unknown for this protein family, but members are found almost always in operons for the the SUF system of iron-sulfur cluster biosynthesis. The SUF system is present elsewhere on the chromosome for those few species where SUF genes are not adjacent. This family shares this property of association with the SUF system with a related family, TIGR02945. TIGR02945 consists largely of a DUF59 domain (see pfam01883), while this protein is about double the length, with a unique N-terminal domain and DUF59 C-terminal domain. A location immediately downstream of the cysteine desulfurase gene sufS in many contexts suggests the gene symbol sufT. Note that some other homologs of this family and of TIGR02945, but no actual members of this family, are found in operons associated with phenylacetic acid (or other ring-hydroxylating) degradation pathways. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312720    2 EEALKDSILGALEMVIDPELGIDIVNLGLVYKVNV----DDEGVCTVDMTLTSMGCPMGPQIIDQVKTVLAEIPEIQDTE 77
Cdd:TIGR03406  71 GEDNEDQVWEQLRTVYDPEIPVNIVDLGLVYGCRVeklgEGQFRVDIEMTLTAPGCGMGPVLVEDVEDKVLAVPNVDEVE 150

                          90       100
                  ....*....|....*....|....
gi 446312720   78 VNIVWSPPWTKDMMSRYAKIALGV 101
Cdd:TIGR03406 151 VELVFDPPWSREMMSEAAKLELGM 174

phenylacetate-CoA oxygenase, PaaJ subunit; Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA. [Energy metabolism, Other]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446312720   16 VIDPEL-GIDIVNLGLVYKVNVDDEGVcTVDMTLTSMGCPMGPQIIDQVKTVLAEIPeIQDTEVNIVWSPPWTKDMMSRY 94
Cdd:TIGR02159   1 VPDPEIpVVSVTDLGMVREVDVDGGGV-VVKFTPTYSGCPALEVIRQDIRDAVRALG-VEVVEVSTSLDPPWTTDWITED 78

                  ..
gi 446312720   95 AK 96
Cdd:TIGR02159  79 AR 80