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
//