ID Q4A0R0_STAS1 Unreviewed; 437 AA.
AC Q4A0R0;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:BAE17332.1};
GN OrderedLocusNames=SSP0187 {ECO:0000313|EMBL:BAE17332.1};
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451 {ECO:0000313|EMBL:BAE17332.1, ECO:0000313|Proteomes:UP000006371};
RN [1] {ECO:0000313|EMBL:BAE17332.1, ECO:0000313|Proteomes:UP000006371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41
RC {ECO:0000313|Proteomes:UP000006371};
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008934; BAE17332.1; -; Genomic_DNA.
DR RefSeq; WP_011302182.1; NZ_MTGA01000037.1.
DR AlphaFoldDB; Q4A0R0; -.
DR KEGG; ssp:SSP0187; -.
DR PATRIC; fig|342451.11.peg.193; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_9; -.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000006371; Chromosome.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
DR CDD; cd00610; OAT_like; 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; IPR004632; 4NH2But_aminotransferase_bac.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00700; GABAtrnsam; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aminotransferase {ECO:0000313|EMBL:BAE17332.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000006371};
KW Transferase {ECO:0000313|EMBL:BAE17332.1}.
SQ SEQUENCE 437 AA; 47891 MW; 0CA081F8B4925961 CRC64;
MSEKYEYYKT QREKYVARGV GNGNLHVADE AQSATVKDVE GNVFIDFAGA IGTLNVGHSH
PEITKHLKAQ LDKFIHPGFN VIMYESYLNL AQKLTEITPG HFDKKSILLN SGAEAVENAV
KIARKYTGRQ AVVSFVRGFH GRTNLTMSMT SKVKPYKLGF GPFAPEVYQA PYPNISEKSE
DLSDELYTQH IINKLHDFFI ETVDPSEVSC IVMEPVQGEG GFIIPDIQFV KAVKQICEDN
GIVFVADEIQ SGFARTGKTF AIEHFDVEPD LITVSKSLAA GFPLSGVVGR KEIVDSASPG
ELGGTYAGNP LACEAALKVI EIIENEDLNG KAEQLGHQLE AYLTALSQDY EQVKAIRRLG
AMVAFEVVDP ETGEPDKALT AKIIKTANEK GLLLLSAGIK GNVIRFLPPL VITDQELNKG
LNILTEVFEK AIEKQTN
//
