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Database: UniProt/TrEMBL
Entry: U5NCR4_9BURK
LinkDB: U5NCR4_9BURK
Original site: U5NCR4_9BURK 
ID   U5NCR4_9BURK            Unreviewed;       367 AA.
AC   U5NCR4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-SEP-2017, entry version 31.
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:AGX87954.1};
GN   ORFNames=Cenrod_1874 {ECO:0000313|EMBL:AGX87954.1};
OS   Candidatus Symbiobacter mobilis CR.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae.
OX   NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX87954.1, ECO:0000313|Proteomes:UP000017184};
RN   [1] {ECO:0000313|EMBL:AGX87954.1, ECO:0000313|Proteomes:UP000017184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR {ECO:0000313|EMBL:AGX87954.1};
RX   PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA   Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA   Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P.,
RA   Rohde M., Overmann J., Bryant D.A.;
RT   "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT   phototrophic consortium "Chlorochromatium aggregatum".";
RL   Genome Biol. 14:R127-R127(2013).
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; CP004885; AGX87954.1; -; Genomic_DNA.
DR   RefSeq; WP_022774508.1; NC_022576.1.
DR   ProteinModelPortal; U5NCR4; -.
DR   EnsemblBacteria; AGX87954; AGX87954; Cenrod_1874.
DR   KEGG; cbx:Cenrod_1874; -.
DR   PATRIC; fig|946483.4.peg.1891; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000017184; 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:UP000017184};
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:UP000017184}.
FT   DOMAIN      233    366       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    254    254       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     130    130       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     302    302       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   367 AA;  39525 MW;  8D8808D1C253635A CRC64;
     MPRPISATIH HAALRHNLLR CRSAAPDSKV WAVIKANAYG HGIERVHEAL RGADGFALLD
     LDEAQRVRGL GWRGPILLIE GVFEPRDLEL CCELRLWHTI HCHAQIDMLA AHKTRTAHHV
     FLKMNSGMNR LGFPANQFRA AWARLHALTQ VGEISLMTHF SDADVPGGTQ RQRSTFDVAA
     CDLPGERSLD NSAAMLAGDL APSCEWVRPG ILLYGSAPDY PAHTIADHAL LPTMTLASRV
     IAVQDLVAGD TVGYGSTFVA QAPMRIGIVA CGYADGYPRH APTDTPVLVG GHRTRLLGRV
     SMDMLAVDLT ALREEGHDAG MGSEVVLWGC ASNGAILGID EVAHAAGTVG YELMCALSLR
     VPVRVDA
//
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