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Database: UniProt/TrEMBL
Entry: D1B5S3_THEAS
LinkDB: D1B5S3_THEAS
Original site: D1B5S3_THEAS 
ID   D1B5S3_THEAS            Unreviewed;       380 AA.
AC   D1B5S3;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-SEP-2017, entry version 69.
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=Taci_1132 {ECO:0000313|EMBL:ACZ19364.1};
OS   Thermanaerovibrio acidaminovorans (strain ATCC 49978 / DSM 6589 /
OS   Su883) (Selenomonas acidaminovorans).
OC   Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae;
OC   Thermanaerovibrio.
OX   NCBI_TaxID=525903 {ECO:0000313|EMBL:ACZ19364.1, ECO:0000313|Proteomes:UP000002030};
RN   [1] {ECO:0000313|EMBL:ACZ19364.1, ECO:0000313|Proteomes:UP000002030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49978 / DSM 6589 / Su883
RC   {ECO:0000313|Proteomes:UP000002030};
RA   Chovatia M., Sikorski J., Schroder M., Lapidus A., Nolan M., Tice H.,
RA   Glavina Del Rio T., Copeland A., Cheng J.F., Lucas S., Chen F.,
RA   Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Chain P., Saunders E., Detter J.C.,
RA   Brettin T., Rohde M., Goker M., Spring S., Bristow J., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Eisen J.A.;
RT   "Complete genome sequence of Thermanaerovibrio acidaminovorans type
RT   strain (Su883).";
RL   Stand. Genomic Sci. 1:254-261(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; CP001818; ACZ19364.1; -; Genomic_DNA.
DR   RefSeq; WP_012869879.1; NC_013522.1.
DR   RefSeq; YP_003317646.1; NC_013522.1.
DR   ProteinModelPortal; D1B5S3; -.
DR   STRING; 525903.Taci_1132; -.
DR   EnsemblBacteria; ACZ19364; ACZ19364; Taci_1132.
DR   GeneID; 8630980; -.
DR   KEGG; tai:Taci_1132; -.
DR   PATRIC; fig|525903.6.peg.1131; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; TACI525903:GH4K-1156-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002030; 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:UP000002030};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ACZ19364.1};
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:UP000002030}.
FT   DOMAIN      242    370       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     36     36       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     134    134       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      36     36       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   380 AA;  41739 MW;  CC6935895A77F763 CRC64;
     MLRPTRMEVS LRAVRHNLDQ IRSYVGGRAQ VMGVVKANAY GLGARRVVEA LRAQGVVRFA
     VATPDEAVQL REWGVGEPVL VLGQCLPSAA GEMVAMDVTC AVGSLELARA LSAEAERQGR
     QVKVHIKVDT GMGRIGFLPG ELEAAMDQIL SMRHLDVEGI FTHFATADEA RLDHAEEQLR
     RFGDALDRMR CRGVRFRLRH ACNSAATIRM PHGHLDAVRP GIILYGMRPS PLCPMPLNLE
     VPFEVNTAVA AVRELPPMWG ISYGMRYVTR GNERIAVLPI GYRDGYARAL SGKAQVLIRG
     RRFPVVGTIC MDQCMVDVTD CPSVQVGDPV VLLGRQGDQA ITPEEFASWL NTIVYEVPGM
     FSERVPRVYV DREGEGPGEG
//
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