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Database: UniProt/TrEMBL
Entry: A0A0X8R504_9SPHN
LinkDB: A0A0X8R504_9SPHN
Original site: A0A0X8R504_9SPHN 
ID   A0A0X8R504_9SPHN        Unreviewed;       379 AA.
AC   A0A0X8R504;
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   Name=alr {ECO:0000313|EMBL:AMG75271.1};
GN   ORFNames=SGRAN_2923 {ECO:0000313|EMBL:AMG75271.1};
OS   Sphingopyxis granuli.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=267128 {ECO:0000313|EMBL:AMG75271.1, ECO:0000313|Proteomes:UP000058599};
RN   [1] {ECO:0000313|EMBL:AMG75271.1, ECO:0000313|Proteomes:UP000058599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFA {ECO:0000313|EMBL:AMG75271.1,
RC   ECO:0000313|Proteomes:UP000058599};
RX   PubMed=26847793; DOI=10.1186/s12864-016-2411-1;
RA   Garcia-Romero I., Perez-Pulido A.J., Gonzalez-Flores Y.E.,
RA   Reyes-Ramirez F., Santero E., Floriano B.;
RT   "Genomic analysis of the nitrate-respiring Sphingopyxis granuli
RT   (formerly Sphingomonas macrogoltabida) strain TFA.";
RL   BMC Genomics 17:93-93(2016).
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; CP012199; AMG75271.1; -; Genomic_DNA.
DR   EnsemblBacteria; AMG75271; AMG75271; SGRAN_2923.
DR   KEGG; sgi:SGRAN_2923; -.
DR   PATRIC; fig|267128.3.peg.3083; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000058599; 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:UP000058599};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AMG75271.1};
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:UP000058599}.
FT   DOMAIN      242    368       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     42     42       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    263    263       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     141    141       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     311    311       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      42     42       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   379 AA;  40220 MW;  3F9E025D65465F7B CRC64;
     MPDNRAPTAR CGRLWIDLSA LARNYAAIAA RVAPATAAAV VKADAYGLGS GPVASALWDA
     GCRRFFVAHL DEALAIRDEL PPQAELIVLN GLPPGVEPLC ARHEIVPVLN SLGQAERWAE
     TARALDRRLP AVLQLDSGMS RLGLAPEDDV RLAHDDRFRQ AVDLRLVMSH LASSGTPGSE
     ANAMQIAAFD RLAAAFPGIP RSLANSGGAF LAAPYHKDVV RAGIALYGGS PSGDPADALE
     PVVRLDARVV QVRTVPEGTG VGYDLTHRCT RPTRIATIGV GYADGLPRTL GNRGAAWFDG
     RRLPILGRVS MDSITLDVSD LPAGQPAEGD WVEIIGPHQP VDVLARDAGT ISYEILTSLG
     HRYDRHYLPF AGVNSGRPA
//
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