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Database: UniProt/TrEMBL
Entry: A0A109QY86_9MICO
LinkDB: A0A109QY86_9MICO
Original site: A0A109QY86_9MICO 
ID   A0A109QY86_9MICO        Unreviewed;       409 AA.
AC   A0A109QY86;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-SEP-2017, entry version 13.
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=AWU67_15435 {ECO:0000313|EMBL:AMB60020.1};
OS   Microterricola viridarii.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Microterricola.
OX   NCBI_TaxID=412690 {ECO:0000313|EMBL:AMB60020.1, ECO:0000313|Proteomes:UP000058305};
RN   [1] {ECO:0000313|EMBL:AMB60020.1, ECO:0000313|Proteomes:UP000058305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS5:02 {ECO:0000313|EMBL:AMB60020.1,
RC   ECO:0000313|Proteomes:UP000058305};
RA   Kumar R., Singh D., Swarnkar M.K.;
RT   "First complete genome sequence of a species in the genus
RT   Microterricola, an extremophilic cold active enzyme producing strain
RT   ERGS5:02 isolated from Sikkim Himalaya.";
RL   Submitted (JAN-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; CP014145; AMB60020.1; -; Genomic_DNA.
DR   EnsemblBacteria; AMB60020; AMB60020; AWU67_15435.
DR   KEGG; mvd:AWU67_15435; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000058305; 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 {ECO:0000313|Proteomes:UP000058305};
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:UP000058305}.
FT   DOMAIN      280    408       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     72     72       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    301    301       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     170    170       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     349    349       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      72     72       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   409 AA;  42497 MW;  77680855D7ACF761 CRC64;
     MGHRARPGHR QAAGPADDDR CRGPADRPLQ PAAMSGAAEP AVVATIDLAA IRHNVALLRQ
     RAGGAAVMVV VKADGYGHGA AECARAALQA GAREVGVATI DEALALRRAG IRAPILAWLH
     ASDAQFRAAL EADIALGVSS LAQARAVRAI AATLGRPVRV DLKLDTGLAR NGAQAEQWAP
     IMRELAAAER EGGLRVHGLF SHLARADEPL HPLIDEQAAR FRQGVALARR LGLAPTANHL
     ANSAAALTRP DLAFDLVRAG IASYGLSPIP QLGDLGLRPA LSLGARIALT KRIGAGDGVS
     YGHAWTAERA GTVALVPMGY ADGLPRALSG RFSVRIGGRR YPAVGRICMD QFLVDLGDNP
     DGIQAGETAT LLGPSALDGT LQGWADELGT ISYELATLLR GRTARAYAG
//
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