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Database: UniProt/TrEMBL
Entry: A0A031K0V2_9SPHN
LinkDB: A0A031K0V2_9SPHN
Original site: A0A031K0V2_9SPHN 
ID   A0A031K0V2_9SPHN        Unreviewed;       372 AA.
AC   A0A031K0V2;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-SEP-2017, entry version 27.
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=BES08_19720 {ECO:0000313|EMBL:AOR79120.1}, BV97_01597
GN   {ECO:0000313|EMBL:EZP82673.1};
OS   Novosphingobium resinovorum.
OG   Plasmid pSA1 {ECO:0000313|EMBL:AOR79120.1,
OG   ECO:0000313|Proteomes:UP000094626}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=158500 {ECO:0000313|EMBL:EZP82673.1, ECO:0000313|Proteomes:UP000024329};
RN   [1] {ECO:0000313|EMBL:EZP82673.1, ECO:0000313|Proteomes:UP000024329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KF1 {ECO:0000313|EMBL:EZP82673.1,
RC   ECO:0000313|Proteomes:UP000024329};
RA   Gan H.M., Gan H.Y., Chew T.H., Savka M.A.;
RT   "Whole genome sequence of Novosphingobium resinovorum KF1.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AOR79120.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA1 {ECO:0000313|EMBL:AOR79120.1};
RC   PLASMID=pSA1 {ECO:0000313|EMBL:AOR79120.1};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000094626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA1 {ECO:0000313|Proteomes:UP000094626};
RX   PubMed=27851894; DOI=10.1016/j.jbiotec.2016.11.013;
RA   Hegedus B., Kos P.B., Balint B., Maroti G., Gan H.M., Perei K.,
RA   Rakhely G.;
RT   "Complete genome sequence of Novosphingobium resinovorum SA1, a
RT   versatile xenobiotic-degrading bacterium capable of utilizing
RT   sulfanilic acid.";
RL   J. Biotechnol. 241:76-80(2017).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|SAAS:SAAS00630646}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; CP017076; AOR79120.1; -; Genomic_DNA.
DR   EMBL; JFYZ01000005; EZP82673.1; -; Genomic_DNA.
DR   RefSeq; WP_008828690.1; NZ_JFYZ01000005.1.
DR   EnsemblBacteria; AOR79120; AOR79120; BES08_19720.
DR   EnsemblBacteria; EZP82673; EZP82673; BV97_01597.
DR   KEGG; nre:BES08_19720; -.
DR   PATRIC; fig|158500.4.peg.1635; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000024329; Unassembled WGS sequence.
DR   Proteomes; UP000094626; Plasmid pSA1.
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 {ECO:0000313|Proteomes:UP000024329,
KW   ECO:0000313|Proteomes:UP000094626};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:EZP82673.1};
KW   Plasmid {ECO:0000313|EMBL:AOR79120.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      233    359       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    254    254       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     134    134       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     302    302       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   372 AA;  39275 MW;  64962C9837D0CC63 CRC64;
     MITAARLTID LEALAANYRL IRDRVVPAQT GGVVKADGYG LGAVTVARTL MAEGCRHLFV
     ALFSEAEALM PQLESGAEVY VLNGLLPGLE PRCAGLGAIP VLNSLDQVSR WSAQARQSGL
     ALPAVLQIDT GMSRMGLPPE EVEHLIATPA LLDGIELRFL ISHLACADDP EDPANAAQEA
     LFNTIAARFP QVPRALDNSG GTFHRRGHFD LVRAGIALYG GNPGTGPNPM QPVVGLEAPI
     AQLRTIPAGT GVGYGLTFHA ARETRIATIP VGYADGWPRC LGNRGAAYVA GVRAPIVGRV
     SMDSITLDVT DVPAGHLYPG APVELIGPNQ SLDQVAADAG TISYEILTQL SRRYDRDYLP
     VRAPALDRST IA
//
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