ID E4U4J0_OCEP5 Unreviewed; 358 AA.
AC E4U4J0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
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=Ocepr_1530 {ECO:0000313|EMBL:ADR36983.1};
OS Oceanithermus profundus (strain DSM 14977 / NBRC 100410 / VKM B-2274 /
OS 506).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Oceanithermus.
OX NCBI_TaxID=670487 {ECO:0000313|EMBL:ADR36983.1, ECO:0000313|Proteomes:UP000008722};
RN [1] {ECO:0000313|Proteomes:UP000008722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14977 / NBRC 100410 / VKM B-2274 / 506
RC {ECO:0000313|Proteomes:UP000008722};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Zhang X., Brettin T.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Faehnrich R.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete sequence of chromosome of Oceanithermus profundus DSM
RT 14977.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADR36983.1, ECO:0000313|Proteomes:UP000008722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14977 / NBRC 100410 / VKM B-2274 / 506
RC {ECO:0000313|Proteomes:UP000008722};
RX PubMed=21677858; DOI=10.4056/sigs.1734292;
RA Pati A., Zhang X., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H.,
RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Hauser L.,
RA Jeffries C.D., Brambilla E.M., Rohl A., Mwirichia R., Rohde M.,
RA Tindall B.J., Sikorski J., Wirth R., Goker M., Woyke T., Detter J.C.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Land M.;
RT "Complete genome sequence of Oceanithermus profundus type strain (506).";
RL Stand. Genomic Sci. 4:210-220(2011).
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; CP002361; ADR36983.1; -; Genomic_DNA.
DR RefSeq; WP_013458153.1; NC_014761.1.
DR AlphaFoldDB; E4U4J0; -.
DR STRING; 670487.Ocepr_1530; -.
DR KEGG; opr:Ocepr_1530; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_2_2_0; -.
DR OrthoDB; 9813814at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000008722; 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:UP000008722}.
FT DOMAIN 229..355
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 34
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 250
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 34
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 358 AA; 37931 MW; 72D4448434D4408E CRC64;
MRPTWLEIDL GALGRNCAHL AGRAPDAQLI AVVKADAYGH GAVRVARYLR ERCGVRRFAV
ATSGEGAELR AAGIAEPVLL LGALHPDDAE GAARHGLTPT LVTLAAARAF AAARPGGRVQ
VKVDSGMGRV GVAPAELAGF MAAVEGLGLE VEAIYTHFAV ADEDEAETRR QLAVFLEAAR
ALPRRYPLHA ANSAAILAGL GTGLDFVRPG VALYGLPPDM KEAPGLEPVL AWKARPTQVK
RLPAGHGVGY GLSYRAGGEE WIATLPFGYA DGFSRALSNR GWVRWRGGYA PVAGRVSMDQ
TTVRLPEPVG LDEVFEVVTP DLDERTGLTG RARALGTIHY ELATALSRRL PRIYLGDG
//
