ID A0A0Q9KVR5_9BACL Unreviewed; 387 AA.
AC A0A0Q9KVR5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Aminotransferase class V domain-containing protein {ECO:0000259|Pfam:PF00266};
GN ORFNames=ASG81_16335 {ECO:0000313|EMBL:KRE41679.1};
OS Paenibacillus sp. Soil522.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736388 {ECO:0000313|EMBL:KRE41679.1, ECO:0000313|Proteomes:UP000051180};
RN [1] {ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|Proteomes:UP000051180};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE41679.1, ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|EMBL:KRE41679.1,
RC ECO:0000313|Proteomes:UP000051180};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64428; EC=2.8.1.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001357};
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:KRE41679.1}.
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DR EMBL; LMRV01000049; KRE41679.1; -; Genomic_DNA.
DR RefSeq; WP_056636346.1; NZ_LMRV01000049.1.
DR AlphaFoldDB; A0A0Q9KVR5; -.
DR STRING; 1736388.ASG81_16335; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000051180; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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}.
FT DOMAIN 4..370
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 387 AA; 42284 MW; 8606E769F028164B CRC64;
MDGTYFDYNA TTPIDPSVSH AMIEHLSLYG NPSSNHQAGR SARAAVQDAR EQAAALLNCK
ASELHFTSGG SESNNWAVKG WLSQWKGTRP HVITSSIEHS SVLEVLHYAA RECGVDVTYL
PVNAEGYVCA EAVATALREE TRMISIMLAN NELGTIQPIR EIARIARSNH IFMHTDAVQA
VGKINVDVQE LGVHALSFSS HKFYGPKGVD GIYLSSGYQL EPLVHGGGQE SGMRSGTENV
LSLIGLSEAC RLARAETAET EQRLAGYKLL LEKRLKKLSP QIRINGSMDA ARTLSNTMNI
QIPNIRGEAL AAYLDHRFGI AVSVGSACSS NQEKKLSGVL MATGLTEAEI QTSIRISMGK
FTRREDLDYF IDSIEQALEH FYRLMPA
//