ID G2J0H9_PSEUL Unreviewed; 355 AA.
AC G2J0H9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN Name=alr {ECO:0000313|EMBL:BAK75968.1};
GN OrderedLocusNames=NH8B_1138 {ECO:0000313|EMBL:BAK75968.1};
OS Pseudogulbenkiania sp. (strain NH8B).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Pseudogulbenkiania.
OX NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK75968.1, ECO:0000313|Proteomes:UP000001274};
RN [1] {ECO:0000313|Proteomes:UP000001274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274};
RX PubMed=22038961; DOI=10.1128/JB.06127-11;
RA Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.;
RT "Complete genome sequence of the denitrifying and N(2)O-reducing bacterium
RT Pseudogulbenkiania sp. strain NH8B.";
RL J. Bacteriol. 193:6395-6396(2011).
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; AP012224; BAK75968.1; -; Genomic_DNA.
DR RefSeq; WP_014086396.1; NC_016002.1.
DR AlphaFoldDB; G2J0H9; -.
DR STRING; 748280.NH8B_1138; -.
DR KEGG; pse:NH8B_1138; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_1_0_4; -.
DR OMA; WEILCGF; -.
DR OrthoDB; 9813814at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000001274; 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; cd06827; PLPDE_III_AR_proteobact; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001274}.
FT DOMAIN 232..355
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 253
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 301
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 355 AA; 38338 MW; DA83DF449DBBF05D CRC64;
MRPLIASIRL EHFRHNYELA RRQHGGRALA VVKANAYGHG AVRCAQAVAD IADGYAVACL
EEALQLREAG LTLPILLLEG VFEAAELREV EQHGLWLVVQ SQQQLDMLLA SQPAKPYRVW
LKMDSGMHRA GFFPQDYAAA YQRLAESGKV DGIVKMTHFA RADEPALSAT AQQMETFDAA
CAGLPGEVSV ANSAAIMVHE RTRRDWGRPG IMLYGATPLP AGYAQDAALK PVMRLTSRVF
GVRELAAGEP VGYGATFVTE RPSRVGLIAC GYADGYPRLA STGSPVAIDG VRSRIIGRVS
MDMITVDLTD LPAAGIGSEV ELWGDSVNVN EVAAQAGTIA YELLCNVKRA HFVYC
//