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Database: UniProt/TrEMBL
Entry: A0A127A2Q9_9MICC
LinkDB: A0A127A2Q9_9MICC
Original site: A0A127A2Q9_9MICC 
ID   A0A127A2Q9_9MICC        Unreviewed;       381 AA.
AC   A0A127A2Q9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-FEB-2018, entry version 12.
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=SA2016_2812 {ECO:0000313|EMBL:AMM33477.1};
OS   Sinomonas atrocyanea.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Sinomonas.
OX   NCBI_TaxID=37927 {ECO:0000313|EMBL:AMM33477.1, ECO:0000313|Proteomes:UP000070134};
RN   [1] {ECO:0000313|EMBL:AMM33477.1, ECO:0000313|Proteomes:UP000070134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 3377 {ECO:0000313|EMBL:AMM33477.1,
RC   ECO:0000313|Proteomes:UP000070134};
RA   Kim K.M.;
RT   "Complete genome of Sinomonas atrocyanea KCTC 3377.";
RL   Submitted (FEB-2016) 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; CP014518; AMM33477.1; -; Genomic_DNA.
DR   RefSeq; WP_066502584.1; NZ_CP014518.1.
DR   EnsemblBacteria; AMM33477; AMM33477; SA2016_2812.
DR   KEGG; satk:SA2016_2812; -.
DR   PATRIC; fig|37927.3.peg.2888; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000070134; 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; -; 2.
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:UP000070134};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
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:UP000070134}.
FT   DOMAIN      248    377       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     39     39       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    269    269       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     316    316       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      39     39       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   381 AA;  39823 MW;  C2097F4E91896CD1 CRC64;
     MPSTRLPERA AVIDLDAIRH NVGVVRKVAE PARVMAVVKA DGYGHGAVPV ARAALEAGAS
     WLGVAHISEA LALRAAGIDA PILAWLHTPD SNFSAAVAAG IDLGCSGWEL DAIVAAAREQ
     ERPARVHLKI DTGLGRNGVT ADRWEAVVGE AVEYQDEGLL RVAGVFSHLA VADEPERPET
     DAQLDAFREA VALAEDAGCD LDVRHIANSP AIFSRPDAHF DLVRAGISIY GLSPFAEQTS
     ADLHLRPAMT LRATLSQAKR VPADQGVSYG LTYRTASAGA LGLVPLGYAD GVPRTSDRGP
     VRIAGRTYPV AGRVAMDQIV VDLGASADPA ELAGAEAVLF GSGADGGPTA DDWARATGTI
     NYEIVTRISQ RVPRVYVGEG A
//
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