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Database: UniProt/TrEMBL
Entry: H0Q4H3_9RHOO
LinkDB: H0Q4H3_9RHOO
Original site: H0Q4H3_9RHOO 
ID   H0Q4H3_9RHOO            Unreviewed;       372 AA.
AC   H0Q4H3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-SEP-2017, entry version 45.
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:BAL26886.1};
GN   ORFNames=AZKH_p0003 {ECO:0000313|EMBL:BAL26886.1};
OS   Azoarcus sp. KH32C.
OG   Plasmid pAZKH {ECO:0000313|EMBL:BAL26886.1,
OG   ECO:0000313|Proteomes:UP000007106}.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Zoogloeaceae; Azoarcus.
OX   NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL26886.1, ECO:0000313|Proteomes:UP000007106};
RN   [1] {ECO:0000313|EMBL:BAL26886.1, ECO:0000313|Proteomes:UP000007106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH32C {ECO:0000313|EMBL:BAL26886.1,
RC   ECO:0000313|Proteomes:UP000007106};
RC   PLASMID=Plasmid pAZKH {ECO:0000313|Proteomes:UP000007106};
RA   Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S.,
RA   Senoo K.;
RT   "Complete genome sequence of Azoarcus sp. KH32C.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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; AP012305; BAL26886.1; -; Genomic_DNA.
DR   RefSeq; WP_015451663.1; NC_020548.1.
DR   ProteinModelPortal; H0Q4H3; -.
DR   EnsemblBacteria; BAL26886; BAL26886; AZKH_p0003.
DR   KEGG; aza:AZKH_p0003; -.
DR   PATRIC; fig|748247.4.peg.4573; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007106; Plasmid pAZKH.
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:UP000007106};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
KW   Plasmid {ECO:0000313|EMBL:BAL26886.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007106}.
FT   DOMAIN      241    367       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     41     41       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    262    262       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     140    140       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     310    310       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      41     41       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   372 AA;  39603 MW;  47D894B5E61B76BE CRC64;
     MSDQHQTRAG ALLSIDLDAI CDNWRSLKGR LGAAACAAVV KADAYGLGAI QVGPALYGAG
     CRHFFVAHLN EAIELRPFLP TDAALYVLHG AHPGAEGEFV RHRLVPVLNS LPQLTAWQKL
     ARELDTVLPG VLQVDSGMAR LGLSEDELAI VASDHGRLQG IELKFIMSHL VSAEDQANPA
     NMIQLANFRA ALQRLPAARA SLANSSGIFL GNDFHFNLAR PGAALYGVAP VAGQPNPMRP
     VIRLQGKVLQ TRRIETGTAV GYSHTWRAAR PSRIATVAVG YADGYLRSLS NRGHAGFEGI
     RLPIVGNVSM DTITIDVTEV PAGRLGEGSL IDLADPLNGV DEMAGRAGTI GYEILTSLGN
     RYARRYIGAV DA
//
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