ID G5JG46_9STAP Unreviewed; 380 AA.
AC G5JG46;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Aminotransferase, class V {ECO:0000313|EMBL:EHJ08845.1};
GN ORFNames=SS7213T_02053 {ECO:0000313|EMBL:EHJ08845.1};
OS Staphylococcus simiae CCM 7213 = CCUG 51256.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=911238 {ECO:0000313|EMBL:EHJ08845.1, ECO:0000313|Proteomes:UP000005413};
RN [1] {ECO:0000313|EMBL:EHJ08845.1, ECO:0000313|Proteomes:UP000005413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 7213 {ECO:0000313|EMBL:EHJ08845.1,
RC ECO:0000313|Proteomes:UP000005413};
RX PubMed=22272658; DOI=10.1186/1471-2164-13-38;
RA Suzuki H., Lefebure T., Pavinski Bitar P., Stanhope M.J.;
RT "Comparative genomic analysis of the genus Staphylococcus including
RT Staphylococcus aureus and its newly described sister species Staphylococcus
RT simiae.";
RL BMC Genomics 13:38-38(2012).
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:EHJ08845.1}.
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DR EMBL; AEUN01000039; EHJ08845.1; -; Genomic_DNA.
DR RefSeq; WP_002462072.1; NZ_AEUN01000039.1.
DR AlphaFoldDB; G5JG46; -.
DR PATRIC; fig|911238.3.peg.380; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000005413; 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 GO; GO:0008483; F:transaminase activity; 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 Aminotransferase {ECO:0000313|EMBL:EHJ08845.1};
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};
KW Transferase {ECO:0000313|EMBL:EHJ08845.1}.
FT DOMAIN 3..364
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 380 AA; 42597 MW; C8127C9D49EDA550 CRC64;
MEIYADYAAT TPVKPEVIDV MTKMYQTHYG NPSSIHTIGR DARKYLDQSR RQIAQILGAK
PNEIIFTSGA TESNNTAIKG IVKANEQLGN HIITSKIEHH SVLHVFEQLE KEGYDVTYLD
VDDTGAIDLD QLAETINDQT ILVSIMFVNN EVGTVQQIYD IEDIIADTHA FFHVDAVQAI
GHLDIKFEDF NIDAMSITAH KFGGPKGVGA LLIKDHLPID FMQLGGEQEF KRRAGTENLP
QIVGMAKALE LADENRDNNN LHLMNLKEQF LVKLQERAIP FELNGSMTSS TGHIVNLYFP
FIEVETMLTL LDLAHIYVSS GSACTAGSTQ PSHVLAAMYE DEERAHHSIR FSFNELTTED
DINNIVAEIH KIYFKFKEES
//
