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Database: UniProt/TrEMBL
Entry: K9W8L6_9CYAN
LinkDB: K9W8L6_9CYAN
Original site: K9W8L6_9CYAN 
ID   K9W8L6_9CYAN            Unreviewed;       406 AA.
AC   K9W8L6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-SEP-2017, entry version 36.
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=Mic7113_0212 {ECO:0000313|EMBL:AFZ16146.1};
OS   Microcoleus sp. PCC 7113.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Microcoleus.
OX   NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ16146.1, ECO:0000313|Proteomes:UP000010471};
RN   [1] {ECO:0000313|EMBL:AFZ16146.1, ECO:0000313|Proteomes:UP000010471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ16146.1,
RC   ECO:0000313|Proteomes:UP000010471};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A.,
RA   Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Pagani I., Pati A., Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X.,
RA   Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
RL   Submitted (JUN-2012) 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; CP003630; AFZ16146.1; -; Genomic_DNA.
DR   RefSeq; WP_015180310.1; NC_019738.1.
DR   ProteinModelPortal; K9W8L6; -.
DR   EnsemblBacteria; AFZ16146; AFZ16146; Mic7113_0212.
DR   KEGG; mic:Mic7113_0212; -.
DR   PATRIC; fig|1173027.3.peg.232; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; MSP1173027:GLGJ-207-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000010471; 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:UP000010471};
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:UP000010471}.
FT   DOMAIN      272    400       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     65     65       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    293    293       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     164    164       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     341    341       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      65     65       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   406 AA;  44640 MW;  D37E6AC071706EE2 CRC64;
     MRQKLKQTNG VTYRQIESDF PRTDKGFSDL CQRAWVEINQ GALSHNVGQL RKLLSASTQL
     MAVVKADAYG HGATMVARIA LEAGAHGLCV ATLQEGIQLR EAGIEAPILL LGAMNTPEQV
     KAIAHWQLEP TICTPQQAWI FSETLSELQK TLPVHLKLDT GMSRLGMPWQ EATQFVELVK
     RLPYLEIASI YSHLATADSP DPTIMRLQHQ RFEEAIAQLR HAGIKPPRLH LANSAATLAD
     SSLHYDWVRA GLALYGLYPA EHLRNAVELH PVMQVKARVT QVKTIPPGTG VSYGYQFIAD
     KETRIAIVGI GYADGVPRNL SNKMTVLIQG QQVRQIGAIT MDQMMLDVSA ISDLETGEVV
     TLIGQDGNLS ISADDWAQTL GTISWEILCS FKHRLPRVAV SDGMLA
//
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