ID A0A0U3BN09_STRGL Unreviewed; 384 AA.
AC A0A0U3BN09;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN ORFNames=WQO_21645 {ECO:0000313|EMBL:ALU98231.1};
OS Streptomyces globisporus C-1027.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1172567 {ECO:0000313|EMBL:ALU98231.1, ECO:0000313|Proteomes:UP000064183};
RN [1] {ECO:0000313|EMBL:ALU98231.1, ECO:0000313|Proteomes:UP000064183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-1027 {ECO:0000313|EMBL:ALU98231.1,
RC ECO:0000313|Proteomes:UP000064183};
RX PubMed=22815456; DOI=10.1128/JB.00797-12;
RA Wang L., Wang S., He Q., Yu T., Li Q., Hong B.;
RT "Draft genome sequence of Streptomyces globisporus C-1027, which produces
RT an antitumor antibiotic consisting of a nine-membered enediyne with a
RT chromoprotein.";
RL J. Bacteriol. 194:4144-4144(2012).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01201};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC Rule:MF_01201}.
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DR EMBL; CP013738; ALU98231.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U3BN09; -.
DR STRING; 1172567.WQO_21645; -.
DR KEGG; sgb:WQO_21645; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000064183; Chromosome.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00430; PLPDE_III_AR; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR HAMAP; MF_01201; Ala_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; IPR020622; Ala_racemase_pyridoxalP-BS.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR00492; alr; 1.
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.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}.
FT DOMAIN 244..371
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 33
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 265
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 33
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 384 AA; 39939 MW; 17A454AEB817EFD1 CRC64;
MRARAEIDLA ALRANVRVLR ERAAGAQLMA VVKSDGYGHG AVPCARAARA AGAAWLGTAT
PHEALALRAA GLDGRIMCWL WTPGGPWREA IEADIDVSAG GMWALREIVA AAQAAGRPAR
VQLKADTGLG RGGCQPADWP ELVGAARDAE RAGHLRITGL WSHFACADEP GHPSIAAQLA
VYRDLVAYAE KEGVEPEVRH LANSPATLTI PEAHFDLVRT GIAMYGISPA PELGTSAELG
LRPVMTLAAA VALVKDAPAG HGVSYGHHYT TPADTTLGLI PVGYADGVPR HASGSGPVLV
GGKVRTVAGR VAMDQFVVDL EGDRPEAGAE AVLFGPGDRG EPTAQDWAEA AGTIAYEIVT
RIGARVPRVY VNETADEVTG GVPR
//
