ID G5GZE8_9FIRM Unreviewed; 381 AA.
AC G5GZE8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Aminotransferase class V domain-containing protein {ECO:0000259|Pfam:PF00266};
GN ORFNames=HMPREF9432_00045 {ECO:0000313|EMBL:EHG26189.1};
OS Selenomonas noxia F0398.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=702437 {ECO:0000313|EMBL:EHG26189.1, ECO:0000313|Proteomes:UP000003175};
RN [1] {ECO:0000313|EMBL:EHG26189.1, ECO:0000313|Proteomes:UP000003175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0398 {ECO:0000313|EMBL:EHG26189.1,
RC ECO:0000313|Proteomes:UP000003175};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Blanton J.M., Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Selenomonas noxia F0398.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
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:EHG26189.1}.
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DR EMBL; ADGH01000002; EHG26189.1; -; Genomic_DNA.
DR RefSeq; WP_006695646.1; NZ_JH376857.1.
DR AlphaFoldDB; G5GZE8; -.
DR STRING; 702437.HMPREF9432_00045; -.
DR GeneID; 84786225; -.
DR PATRIC; fig|702437.3.peg.46; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_0_9; -.
DR Proteomes; UP000003175; 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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 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 6..367
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 381 AA; 40211 MW; 53ABD3FD1A19E9D4 CRC64;
MSSAPIYLDY AATTPLDPRV LEEMMPYLTD IYGNPSSLHA FGQRARRAVM RARAQTAALI
GASPEEIFFT SGGTESDNWA LRGIAEAQRT AGRGAHIVTS SIEHAAVLET CHYSERNGFS
VTYLPVDAAG RVDPSDVEAA LRNETILVSI MTANNEVGTI EPIAEIGALV RAHGILFHTD
AVQAAGHIPL NVNTLNVDAL SFSAHKFCGP KGIGILYVRR GTAIAPLLYG GAQERDMRAG
TENTAAIVGC GCAAEIAGIE MTAENERLSI AAEFLHAKLS AVGGISFHGD RESHLAGILN
FGISGTSQDT MLIRLDLAGF AVSAGSACSA GAAHPSHVLQ AMGLSEPEIR ASIRVSLGRF
TKHEDIVSFA DRIIAIAGEQ Y
//
