ID G2I389_KOMMN Unreviewed; 381 AA.
AC G2I389;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Alanine racemase {ECO:0000256|ARBA:ARBA00013089, ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|ARBA:ARBA00013089, ECO:0000256|HAMAP-Rule:MF_01201};
GN OrderedLocusNames=GLX_02820 {ECO:0000313|EMBL:BAK82694.1};
OS Komagataeibacter medellinensis (strain NBRC 3288 / BCRC 11682 / LMG 1693 /
OS Kondo 51) (Gluconacetobacter medellinensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Komagataeibacter.
OX NCBI_TaxID=634177 {ECO:0000313|EMBL:BAK82694.1, ECO:0000313|Proteomes:UP000009044};
RN [1] {ECO:0000313|Proteomes:UP000009044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3288 / BCRC 11682 / LMG 1693
RC {ECO:0000313|Proteomes:UP000009044};
RX PubMed=22123756; DOI=10.1128/JB.06158-11;
RA Ogino H., Azuma Y., Hosoyama A., Nakazawa H., Matsutani M., Hasegawa A.,
RA Otsuyama K., Matsushita K., Fujita N., Shirai M.;
RT "Complete genome sequence of NBRC 3288, a unique cellulose-nonproducing
RT strain of Gluconacetobacter xylinus isolated from vinegar.";
RL J. Bacteriol. 193:6997-6998(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|ARBA:ARBA00000316, ECO:0000256|HAMAP-
CC 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.
CC {ECO:0000256|ARBA:ARBA00007880, ECO:0000256|HAMAP-Rule:MF_01201}.
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DR EMBL; AP012159; BAK82694.1; -; Genomic_DNA.
DR RefSeq; WP_014104274.1; NC_016027.1.
DR AlphaFoldDB; G2I389; -.
DR STRING; 634177.GLX_02820; -.
DR KEGG; gxy:GLX_02820; -.
DR PATRIC; fig|634177.7.peg.313; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_1_1_5; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000009044; 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 250..377
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 50
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 271
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 50
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 381 AA; 40051 MW; 5B8AF4039D2AC0DE CRC64;
MTNLPFPTPA TGWAAPGAGA MLEISLGAIA ANYRLLNARA GQATCAAVVK ADAYGLGAHK
VAPVLEQAGA KVFFVAHLEE GIRLRAHVSP AAEIFVLHGP MPGTEQEFTR HALLPVLNSM
EQIAGWHAHA TQTQQALPAA IQVDTGMSRF GLSEADVAIL AATPALLEGI DTRLVMSHLA
CADTPDNPAN AMQRDRLRAM AALLPAAPLA LSASSGIFLG PDYHFDLVRP GAALYGLAPN
ADAPNPLHPT VRLQARIVQR RTIGAGNGVG YGLTWRASGP KRIATLGIGY ADGFLRQGAN
NGGCAWLDSY RLPILGRISM DSTTIDVSDV PESVLDQITH VDMIGPHRSV DDVAHSAGTI
GYEVLTALGS RFHRAYLPQV A
//
