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Database: UniProt/TrEMBL
Entry: I4BUV4_ACEMN
LinkDB: I4BUV4_ACEMN
Original site: I4BUV4_ACEMN 
ID   I4BUV4_ACEMN            Unreviewed;       376 AA.
AC   I4BUV4;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-SEP-2017, entry version 41.
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=Anamo_0404 {ECO:0000313|EMBL:AFM21061.1};
OS   Acetomicrobium mobile (strain ATCC BAA-54 / DSM 13181 / NGA)
OS   (Acetomicrobium mobile).
OC   Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae;
OC   Acetomicrobium.
OX   NCBI_TaxID=891968 {ECO:0000313|EMBL:AFM21061.1, ECO:0000313|Proteomes:UP000006061};
RN   [1] {ECO:0000313|Proteomes:UP000006061}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC BAA-54 / DSM 13181 / NGA
RC   {ECO:0000313|Proteomes:UP000006061};
RX   PubMed=23961311; DOI=10.4056/sigs.3547050;
RA   Mavromatis K., Stackebrandt E., Held B., Lapidus A., Nolan M.,
RA   Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A.,
RA   Pitluck S., Liolios K., Pagani I., Ivanova N., Mikhailova N.,
RA   Huntemann M., Pati A., Chen A., Palaniappan K., Land M., Rohde M.,
RA   Spring S., Goker M., Woyke T., Detter J.C., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of the moderate thermophile Anaerobaculum
RT   mobile type strain (NGA(T)).";
RL   Stand. Genomic Sci. 8:47-57(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}.
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}.
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DR   EMBL; CP003198; AFM21061.1; -; Genomic_DNA.
DR   RefSeq; WP_014806299.1; NC_018024.1.
DR   ProteinModelPortal; I4BUV4; -.
DR   EnsemblBacteria; AFM21061; AFM21061; Anamo_0404.
DR   KEGG; amo:Anamo_0404; -.
DR   PATRIC; fig|891968.3.peg.401; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000006061; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006061};
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:UP000006061}.
FT   DOMAIN      243    371       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     37     37       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    264    264       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     135    135       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     312    312       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      37     37       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   376 AA;  41489 MW;  D910B20D96C1A0CB CRC64;
     MNLRPTRYEV NLTNLQHNFN CVRSFVGPNV QVMSVVKANG YGMGIVRIAR ALAEAGCQRF
     AVATPDEAIA LREAGISEPL LVLGPSPYEA AEYYVRHDIA AALTDMAFAH AASQAAQRQA
     KVARLHLKID SGMGRIGFLP EELPGVLAEL KGLPGLDVEG AFTHFATADE INLEYTHWQF
     KRYMKALDIL DEFGVKVRLR HVCNSPATLN VPKYHLDAVR PGLILYGMWP SEHCNKPFDL
     KPVFQVKTDV AALRTLPLGS GVGYGLRYMT RGEERIAILP IGYHDGYPRP LSMRASVLIK
     GVRAPIVGNI CMDQTMVNVT HIPNVKVGDE VVLIGVQGKE RITPEEIAGL LGTINYEVPN
     LFTPRVPRVY LQENIV
//
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