ID Q4A045_STAS1 Unreviewed; 334 AA.
AC Q4A045;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Putative pyridoxal phosphate-dependent acyltransferase {ECO:0000256|ARBA:ARBA00015148};
GN OrderedLocusNames=SSP0428 {ECO:0000313|EMBL:BAE17573.1};
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:BAE17573.1, ECO:0000313|Proteomes:UP000006371};
RN [1] {ECO:0000313|EMBL:BAE17573.1, 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 ECO:0000256|RuleBase:RU003693};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC {ECO:0000256|ARBA:ARBA00005011}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000256|ARBA:ARBA00007970}.
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DR EMBL; AP008934; BAE17573.1; -; Genomic_DNA.
DR RefSeq; WP_011302396.1; NZ_MTGA01000036.1.
DR AlphaFoldDB; Q4A045; -.
DR KEGG; ssp:SSP0428; -.
DR PATRIC; fig|342451.11.peg.433; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_1_9; -.
DR OrthoDB; 9813612at2; -.
DR Proteomes; UP000006371; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_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; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42885:SF2; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:BAE17573.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693};
KW Reference proteome {ECO:0000313|Proteomes:UP000006371};
KW Transferase {ECO:0000313|EMBL:BAE17573.1}.
FT DOMAIN 22..317
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 334 AA; 38333 MW; 31219DFA4CC3146C CRC64;
MIRINKNESP LRPLTEAQLT SIIHHASFNF YPDEEYERFK AGYARYYNLS PDQIIAGNGS
DELIQKLMLI MPEGPALALN PDFFMYQAYA DQVHRPIAFV NADNDLTFNL ENILSRIEAV
QPAFFIMSNP HNPSGKQYNL TFLTAIADKM KNIGGYFVID EAYLDFGDAY TLELQPHVLQ
MRTLSKAFGI AGLRLGVLIG TPETIQLIQS IEHPYPLNTL TLHIALFMFE HIDKTRTFIE
HQRALAVRLR QMFQDNVSDI MKVFPSSTNF VLTKGSAAQS LGLYIEDHGF LPRRYDEPNM
NDYVRYSIAT DDQLDQLEQL IKSWRSQYDI SKET
//
