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Database: UniProt/TrEMBL
Entry: G8R2E3_OWEHD
LinkDB: G8R2E3_OWEHD
Original site: G8R2E3_OWEHD 
ID   G8R2E3_OWEHD            Unreviewed;       822 AA.
AC   G8R2E3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 63.
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=Oweho_1954 {ECO:0000313|EMBL:AEV32933.1};
OS   Owenweeksia hongkongensis (strain DSM 17368 / CIP 108786 / JCM 12287 / NRRL
OS   B-23963 / UST20020801).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Schleiferiaceae;
OC   Owenweeksia.
OX   NCBI_TaxID=926562 {ECO:0000313|EMBL:AEV32933.1, ECO:0000313|Proteomes:UP000005631};
RN   [1] {ECO:0000313|EMBL:AEV32933.1, ECO:0000313|Proteomes:UP000005631}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 17368 / JCM 12287 / NRRL B-23963
RC   {ECO:0000313|Proteomes:UP000005631};
RX   PubMed=23450211; DOI=10.4056/sigs.3296896;
RA   Riedel T., Held B., Nolan M., Lucas S., Lapidus A., Tice H., Del Rio T.G.,
RA   Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S., Liolios K.,
RA   Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Rohde M., Tindall B.J., Detter J.C., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Genome sequence of the orange-pigmented seawater bacterium Owenweeksia
RT   hongkongensis type strain (UST20020801(T)).";
RL   Stand. Genomic Sci. 7:120-130(2012).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC       also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
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DR   EMBL; CP003156; AEV32933.1; -; Genomic_DNA.
DR   RefSeq; WP_014202287.1; NC_016599.1.
DR   AlphaFoldDB; G8R2E3; -.
DR   STRING; 926562.Oweho_1954; -.
DR   KEGG; oho:Oweho_1954; -.
DR   PATRIC; fig|926562.3.peg.1961; -.
DR   eggNOG; COG0770; Bacteria.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_372082_0_0_10; -.
DR   OMA; MVKAFAY; -.
DR   OrthoDB; 9801978at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000005631; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd00430; PLPDE_III_AR; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 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; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR035911; MurE/MurF_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR005863; UDP-N-AcMur_synth.
DR   NCBIfam; TIGR00492; alr; 1.
DR   NCBIfam; TIGR01143; murF; 1.
DR   PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR   PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000005631}.
FT   DOMAIN          695..820
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        490
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        717
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         589
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         766
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         490
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   822 AA;  91953 MW;  3EFF30795E369B47 CRC64;
     MAQLAISKIA ELLNAEFSAL YPSEIVTRIL LDSRQFSSAE GVLFFALRGK NHDGHKYIED
     LVKKGVSHFV VEQMPTQTFD ANFVVVPDSL KALQDLAKHI REQSSAAVIA VTGSNGKTVV
     KEWMGQILQK QFSTCRSPKS YNSQIGVPLS VWELEAKNEF AVFESGISEP DEMEKLEKIL
     QPEIGIFTNI GSAHDANFES NSEKIAEKLK LFKHSKQLVY EANGSNLAKQ IEVFTEERGI
     QLLSWTRENG PADLRIEVKI EEAQTVLIGT MDERTHTLQI PFTDAASIQN AIHCWRLGLE
     LSLDEEEMKK SFAKLNPVEM RLQMKAGSNG NIIINDAYNS DMESLRVALH YLENQAGNRK
     KVLIISELQQ SGLASEELFS RMAEVINRFE LDEIIAIGKD LKNGAFALNS TAIFYPSTKH
     FLKNIYSHSF KQSAILLKGA RSFHFEEISS ALEEKSHQTV LNIYMNRMVY NLNYFRSKLN
     GGTRIMAMVK AFSYGSGTYE IANLLQFHKV DYLGVAYTDE GVALRKAGIS LPILVLNAEP
     SSFHDLVEYN LEPEVYSFHQ LEMLENALKN YNLSEAFKVH LKVETGMHRL GFVEDQLKDL
     AEKLKSHRHI KVASVFSHLA ASDDPEQRDF TLGQVAKLKQ MTDKLKSDLG YSFLRHISNS
     SGISQYPEAH FDMVRLGVGL YGIGSNVEDK KHLNVVSDLM ASVSQVKQLK VGDSVGYGRT
     FVAEKPTTIA VVSIGYADGF RRSLSNGVGE VVISGKRYQV VGRVCMDMVM VDVTGSDVAE
     GDEVEVFGPT ISVYELAQKM DTIPYEVLTG ISSRVKRVYF ME
//
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