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Database: UniProt
Entry: Q3JEJ2
LinkDB: Q3JEJ2
Original site: Q3JEJ2 
ID   ALR_NITOC               Reviewed;         356 AA.
AC   Q3JEJ2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JAN-2019, entry version 82.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=Noc_0224;
OS   Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / NCIMB 11848 /
OS   C-107).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Chromatiaceae; Nitrosococcus.
OX   NCBI_TaxID=323261;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19707 / BCRC 17464 / NCIMB 11848 / C-107;
RX   PubMed=16957257; DOI=10.1128/AEM.00463-06;
RA   Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA   Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M.,
RA   Poret-Peterson A.T., Vergez L.M., Ward B.B.;
RT   "Complete genome sequence of the marine, chemolithoautotrophic,
RT   ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL   Appl. Environ. Microbiol. 72:6299-6315(2006).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       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:0000255|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; CP000127; ABA56754.1; -; Genomic_DNA.
DR   RefSeq; WP_002813537.1; NC_007484.1.
DR   ProteinModelPortal; Q3JEJ2; -.
DR   SMR; Q3JEJ2; -.
DR   STRING; 323261.Noc_0224; -.
DR   EnsemblBacteria; ABA56754; ABA56754; Noc_0224.
DR   KEGG; noc:Noc_0224; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; 859043at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000006838; 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   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 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   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; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    356       Alanine racemase.
FT                                /FTId=PRO_1000066020.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    253    253       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     129    129       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     301    301       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   356 AA;  38205 MW;  9105C5B5B69ABE1F CRC64;
     MNFPQAIIDA SALRHNLQRV RELAPRSQIM AVVKADGYGH GLTRVADVLV AADAFAVARL
     EEATALRQAG HRCPVVLLGG ISDKEQLQLA AAHRLTLVVH EFAQLDLLER VRITSPLPVW
     VKADTGMHRL GFPPQVVAKA IARLRCCPAV ASVVGLMSHL ASADESEDFL TPIQLQTFEG
     IAAPGLLRSM ANSAAVMVYP YAHFDWVRPG LMLYGASPFA HGTGAAVGLK SVMTLQTRLI
     AIHHLRPGDS IGYGATWVCP EAMTVGVAAL GYGDGYPRHA VSGTPVLVNG RPVPLVGRVS
     MDMITLDLRT QPKAKVGDPV IAWGPNLPVE EVARHATTIP YELLCQVTGR VPRTME
//
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