ID G7WHJ9_DESOD Unreviewed; 394 AA.
AC G7WHJ9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
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=Desor_5546 {ECO:0000313|EMBL:AET70920.1};
OS Desulfosporosinus orientis (strain ATCC 19365 / DSM 765 / NCIMB 8382 / VKM
OS B-1628 / Singapore I) (Desulfotomaculum orientis).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=768706 {ECO:0000313|EMBL:AET70920.1, ECO:0000313|Proteomes:UP000006346};
RN [1] {ECO:0000313|Proteomes:UP000006346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC {ECO:0000313|Proteomes:UP000006346};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Pester M.,
RA Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.,
RA Woyke T.;
RT "Complete sequence of Desulfosporosinus orientis DSM 765.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AET70920.1, ECO:0000313|Proteomes:UP000006346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC {ECO:0000313|Proteomes:UP000006346};
RX PubMed=23105050; DOI=10.1128/JB.01392-12;
RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA Ollivier B., Klenk H.P., Spring S., Loy A.;
RT "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT and Desulfosporosinus acidiphilus DSM22704T.";
RL J. Bacteriol. 194:6300-6301(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; CP003108; AET70920.1; -; Genomic_DNA.
DR RefSeq; WP_014187722.1; NC_016584.1.
DR AlphaFoldDB; G7WHJ9; -.
DR STRING; 768706.Desor_5546; -.
DR KEGG; dor:Desor_5546; -.
DR PATRIC; fig|768706.3.peg.5651; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_2_2_9; -.
DR OrthoDB; 9813814at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000006346; 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 CDD; cd00430; PLPDE_III_AR; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 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 NCBIfam; TIGR00492; alr; 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 PRINTS; PR00992; ALARACEMASE.
DR SMART; SM01005; Ala_racemase_C; 1.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000006346}.
FT DOMAIN 241..371
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 35
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 262
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 35
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 394 AA; 43928 MW; 98BB80A10C11587D CRC64;
MAGTWIEVDL DAVAGNYREI VRHLRPQARC MAVVKADAYG LGAVQVALAL ERTGCEAFAV
TKVEEGLILR EHGIKGAILV LGPSTAEEWP KAMEAQLHLT LSELSAITEI NEVCLDLEQE
VSVHIKLETG MGRTGFRFSE LEALAHNLAA ARQLKVMGVY THFARAAQKD KSYTSEQYEL
FKSYTAKLEE LGIHPLWKHV CNSAAFLDYP EWHHDFVRIG TLLIGHYPGP GFSGKLTLAD
PWIAKSKIVH LRKVPKGTYV GYQSIYCTKE ETQLAVIPVG YADGLGIAPH FVPQGWVDFL
KIIIKNFAAL FGIFLSQERV ELRGRTVRVA GKIGMQLTVI DVGLQECTLG DEVKIPLRRT
LANPRIHRKY KQDGRIFAER IMEEGVSAIY PEYS
//
