ID A0A0H2VG75_STAES Unreviewed; 357 AA.
AC A0A0H2VG75;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Putative alanine racemase {ECO:0000313|EMBL:AAO04676.1};
GN OrderedLocusNames=SE_1079 {ECO:0000313|EMBL:AAO04676.1};
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280 {ECO:0000313|EMBL:AAO04676.1, ECO:0000313|Proteomes:UP000001411};
RN [1] {ECO:0000313|EMBL:AAO04676.1, ECO:0000313|Proteomes:UP000001411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200 {ECO:0000313|Proteomes:UP000001411};
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.Q., Ren S.X., Li H.L., Wang Y.X., Fu G., Yang J., Qin Z.Q.,
RA Miao Y.G., Wang W.Y., Chen R.S., Shen Y., Chen Z., Yuan Z.H., Zhao G.P.,
RA Qu D., Danchin A., Wen Y.M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600821-50};
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; AE015929; AAO04676.1; -; Genomic_DNA.
DR RefSeq; NP_764634.1; NC_004461.1.
DR RefSeq; WP_001831203.1; NZ_WBME01000002.1.
DR AlphaFoldDB; A0A0H2VG75; -.
DR GeneID; 50018795; -.
DR KEGG; sep:SE_1079; -.
DR PATRIC; fig|176280.10.peg.1055; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_2_2_9; -.
DR OrthoDB; 9813814at2; -.
DR Proteomes; UP000001411; Chromosome.
DR GO; GO:0008784; F:alanine racemase activity; IEA:InterPro.
DR GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR000821; Ala_racemase.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR011079; Ala_racemase_C.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR Pfam; PF00842; Ala_racemase_C; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR PRINTS; PR00992; ALARACEMASE.
DR SMART; SM01005; Ala_racemase_C; 1.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR600821-50}.
FT DOMAIN 235..357
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 30
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 357 AA; 41631 MW; B618178F01891DBC CRC64;
MTAIWSLDTE AFYQNAVKVK NNEPIMAVVK NNAYHYGLEF AVKTFLKAEI NTFSTTSLNE
AIRVRKIAPE ATIFLMNPVY DFDLVKRYDI HMTLPSLNYY YKYKQDLKGI HVHLEYENLL
HRSGFRNIEE IREVLKDHDQ NNQDKMIISG IWTHFGYADE FDVDEYKMER DAWLNLINTL
LNENYHFDMI HSQNSASYFR ENQMLLPHHT HARVGIALYG SRPYSLINEE RITQSLTVKG
NVIQVRDVNK GDYCGYSFAF EVKNDHTQLA VVDIGYGDGI LKSRAKHEAI INGKRYPIRA
LMMSHMFIEV DDEVHAQDEV ILYNKDIRID EFTFKGVGAN SEQLSAMNHD SLMKEYL
//
