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
//