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Database: UniProt
Entry: A0A0S8B9K2_9BACT
LinkDB: A0A0S8B9K2_9BACT
Original site: A0A0S8B9K2_9BACT 
ID   A0A0S8B9K2_9BACT        Unreviewed;       397 AA.
AC   A0A0S8B9K2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Aminotransferase class V domain-containing protein {ECO:0000259|Pfam:PF00266};
GN   ORFNames=AMS20_02210 {ECO:0000313|EMBL:KPK08280.1};
OS   Gemmatimonas sp. SG8_28.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=1703357 {ECO:0000313|EMBL:KPK08280.1, ECO:0000313|Proteomes:UP000051120};
RN   [1] {ECO:0000313|EMBL:KPK08280.1, ECO:0000313|Proteomes:UP000051120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_28 {ECO:0000313|EMBL:KPK08280.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/IscS subfamily.
CC       {ECO:0000256|ARBA:ARBA00006490}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPK08280.1}.
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DR   EMBL; LJNQ01000022; KPK08280.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8B9K2; -.
DR   PATRIC; fig|1703357.3.peg.2347; -.
DR   Proteomes; UP000051120; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.260.50; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR016454; Cysteine_dSase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          12..374
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   397 AA;  40569 MW;  CD8F6C32A7E82B7D CRC64;
     MPSPTPRSAL LYLDHAATTP VRSEVRDAML PFLSDEQYGN PSSGHAAGRA ARAALDRARR
     GIADALGCEP GDVVFTSGGT EADNLAVIGA ALRARMDDRP FRVIVSRTEH KAVIDAAHAV
     ERLGGEAVFL DVDGEGRVEP QAAADAVRAG AAVLSVMWVN NETGVVQNIP ALAGAAADAG
     VPFHTDAVQA VGKIPCAMDA PIAMLALSAH KIGGPKGIGA LVVRDAGQIT PVLHGGGQQR
     GIRPGTENVA GAVGLATAVE LAVAEREEAM PRVRELRDRL ASGIAAAVPG LAVTGDGAAR
     APHILHVTIP DLDGNALAIH LDQAGIACST GSACSSGQSS PSHVLTAMGV QPERPYAPLR
     LSLSATTGDE AIDEVLRRMP TVIGQVRVLT AALRGST
//
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