ID   B3PK19_CELJU            Unreviewed;       379 AA.
AC   B3PK19;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 104.
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:ACE84020.1};
GN   OrderedLocusNames=CJA_0676 {ECO:0000313|EMBL:ACE84020.1};
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE84020.1, ECO:0000313|Proteomes:UP000001036};
RN   [1] {ECO:0000313|EMBL:ACE84020.1, ECO:0000313|Proteomes:UP000001036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107 {ECO:0000313|EMBL:ACE84020.1,
RC   ECO:0000313|Proteomes:UP000001036};
RX   PubMed=18556790; DOI=10.1128/JB.01701-07;
RA   Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
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, ECO:0000256|HAMAP-
CC         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; CP000934; ACE84020.1; -; Genomic_DNA.
DR   RefSeq; WP_012486346.1; NC_010995.1.
DR   AlphaFoldDB; B3PK19; -.
DR   STRING; 498211.CJA_0676; -.
DR   KEGG; cja:CJA_0676; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_1_1_6; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001036; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001036}.
FT   DOMAIN          251..378
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        49
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        272
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         147
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         49
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   379 AA;  41308 MW;  3ACEF92858320C29 CRC64;
     MIHHPSPDLL PAMITSSGIL TIDLHAICAN WHFLKNQVAP HVDVAAVVKA NAYGLGAVPV
     VRALRKEGCT TFFFATKEEA LASGLNGEHC LKIVLSGVRS GDEPFFVEGQ LTPVLYSLAD
     VQRWNAYAKN CCKRLPCILK VDTGMTRMGM SIEELEAFCE AHASIHIAPL FLMSHLACAD
     TPSHPANQRQ LQLFKQALDI AQVRFPEIKA SLANSAGILL GADWHFDLVR PGAALYGINP
     VSGIPNLLKP VITLSLPVLQ IRSLQHDAYV GYSATHFAKA GSRLAVVAGG YADGIHRTLG
     FKPLAQFNGM AFEAVGRVSM DSCVFDISQC PENRLPQVGD YLEVVNESLS LNFLMERNAS
     LGYEVLNSLG TRFHRIYQE
//