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Database: UniProt/TrEMBL
Entry: A9H9C8_GLUDA
LinkDB: A9H9C8_GLUDA
Original site: A9H9C8_GLUDA 
ID   A9H9C8_GLUDA            Unreviewed;       387 AA.
AC   A9H9C8;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   05-JUL-2017, entry version 81.
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=dadB {ECO:0000313|EMBL:CAP54653.1};
GN   OrderedLocusNames=GDI0710 {ECO:0000313|EMBL:CAP54653.1};
OS   Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 /
OS   PAl5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconacetobacter.
OX   NCBI_TaxID=272568 {ECO:0000313|EMBL:CAP54653.1, ECO:0000313|Proteomes:UP000001176};
RN   [1] {ECO:0000313|EMBL:CAP54653.1, ECO:0000313|Proteomes:UP000001176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49037 / DSM 5601 / PAl5
RC   {ECO:0000313|Proteomes:UP000001176};
RX   PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA   Bertalan M., Albano R., Padua V., Rouws L., Rojas C., Hemerly A.,
RA   Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L.,
RA   Magalhaes V., Alqueres S., Cardoso A., Almeida W., Loureiro M.M.,
RA   Nogueira E., Cidade D., Oliveira D., Simao T., Macedo J., Valadao A.,
RA   Dreschsel M., Freitas F., Vidal M., Guedes H., Rodrigues E.,
RA   Meneses C., Brioso P., Pozzer L., Figueiredo D., Montano H.,
RA   Junior J., Filho G., Flores V., Ferreira B., Branco A., Gonzalez P.,
RA   Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M.,
RA   Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A.,
RA   Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T.,
RA   Kruger W.V., Martins O., Baldani J.I., Ferreira P.C.;
RT   "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT   Gluconacetobacter diazotrophicus Pal5.";
RL   BMC Genomics 10:450-450(2009).
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; AM889285; CAP54653.1; -; Genomic_DNA.
DR   RefSeq; WP_012223326.1; NC_010125.1.
DR   ProteinModelPortal; A9H9C8; -.
DR   EnsemblBacteria; CAP54653; CAP54653; GDI0710.
DR   KEGG; gdi:GDI0710; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001176; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
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:UP000001176};
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:UP000001176}.
FT   DOMAIN      248    377       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     48     48       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     147    147       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     320    320       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      48     48       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   387 AA;  40295 MW;  E1C145445C076AB1 CRC64;
     MLTADPMPAA PSAWTGGILT IDLDAVAANY RILRDRVGPR TICGAAVKAD AYGLGAARIV
     PVLAEAGCHT FFVAHLAEGA AIRPLLGTDA TIFVLNGAMP GTEAALHEHG LVPVLNSLEQ
     IARWRDLARQ AGRDLPAALQ VDSGMSRFGL SDADVDALAA RDGSLAGITP LLVMSHLACA
     DEPAHPANHA QRAAFLRLRA RLPAAPASLA ASSGLFMGSD WHFDMVRPGA ALYGINPTPG
     WPNPMQPVVR LQARIVQTRW IGPGTAVGYG AAFIADRPSR IATLAVGYGD GFPRAAGGHG
     HAVLPERPAA KLPIIGRISM DCLAVDVTDI SDAPLDAGTA LDLIGPHHSI DSAAAAAGTI
     GYELLTGLGA RYHRLYRDDR SRKGCNG
//
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