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Database: UniProt/TrEMBL
Entry: D5UIS2_CELFN
LinkDB: D5UIS2_CELFN
Original site: D5UIS2_CELFN 
ID   D5UIS2_CELFN            Unreviewed;       410 AA.
AC   D5UIS2;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   28-FEB-2018, entry version 56.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=Cfla_2600 {ECO:0000313|EMBL:ADG75488.1};
OS   Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / NCIB 8073 / NRS
OS   134).
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG75488.1, ECO:0000313|Proteomes:UP000000849};
RN   [1] {ECO:0000313|EMBL:ADG75488.1, ECO:0000313|Proteomes:UP000000849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 482 / DSM 20109 / NCIB 8073 / NRS 134
RC   {ECO:0000313|Proteomes:UP000000849};
RX   PubMed=21304688;
RA   Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Goodwin L., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Cellulomonas flavigena type strain
RT   (134).";
RL   Stand. Genomic Sci. 3:15-25(2010).
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; CP001964; ADG75488.1; -; Genomic_DNA.
DR   RefSeq; WP_013117821.1; NC_014151.1.
DR   ProteinModelPortal; D5UIS2; -.
DR   STRING; 446466.Cfla_2600; -.
DR   EnsemblBacteria; ADG75488; ADG75488; Cfla_2600.
DR   KEGG; cfl:Cfla_2600; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; CFLA446466:G1GLJ-2620-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000849; 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; -; 2.
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:UP000000849};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ADG75488.1};
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:UP000000849}.
FT   DOMAIN      261    394       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     49     49       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    282    282       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     148    148       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     335    335       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      49     49       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   410 AA;  41951 MW;  ACD23BCB97DA0DDA CRC64;
     MPTHDPRGER LAGVNDFPAR AVVDLGAVRG NVRALAAHAP TAQVMAVVKA DAYGHGLVPS
     ALAALEGGAT WLGTAQVPEA LHLRRAGVTG ARILTWLYAP GAPLREAVEA DVDLSVASRW
     ALDDVVAAAR EAGRTARVHL KVDTGLGRNG LVPAQLPEVL TAALAAEAEG VVRVVGVWSH
     LAFADAPDHA VVAQQAGVFA EAVAAVEAAG ARLEVRHLAN SAATLTSPAL HWDLVRPGIA
     VYGLSPVPQL GGPERFGLVP AMTFEAQLAT VKPVPAGSGV SYGHEYVVPH DTVLGVVPVG
     YADGVPRHAS GSAERWGGPV QVGGRRLGVA GRVCMDQVVL DLGPGATESA GDRVVLWGDG
     RDGGPTAQDW ADVAGTISYE LVTRLGARVP RTYVDSARVA APAPSEGGGA
//
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