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Database: UniProt/TrEMBL
Entry: D5EVJ7_PRER2
LinkDB: D5EVJ7_PRER2
Original site: D5EVJ7_PRER2 
ID   D5EVJ7_PRER2            Unreviewed;       792 AA.
AC   D5EVJ7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-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=PRU_0131 {ECO:0000313|EMBL:ADE81691.1};
OS   Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=264731 {ECO:0000313|EMBL:ADE81691.1, ECO:0000313|Proteomes:UP000000927};
RN   [1] {ECO:0000313|EMBL:ADE81691.1, ECO:0000313|Proteomes:UP000000927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000313|Proteomes:UP000000927};
RX   PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RG   North American Consortium for Rumen Bacteria;
RA   Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA   Coutinho P.M., Henrissat B., Nelson K.E.;
RT   "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT   bryantii: insights into their environmental niche.";
RL   Microb. Ecol. 60:721-729(2010).
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; CP002006; ADE81691.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5EVJ7; -.
DR   STRING; 264731.PRU_0131; -.
DR   KEGG; pru:PRU_0131; -.
DR   eggNOG; COG0770; Bacteria.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_372082_0_0_10; -.
DR   OMA; MVKAFAY; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000927; Chromosome.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
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: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   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; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR035911; MurE/MurF_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   NCBIfam; TIGR00492; alr; 1.
DR   PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW   Ligase {ECO:0000313|EMBL:ADE81691.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000000927}.
FT   DOMAIN          666..790
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        462
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        687
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         560
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         736
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         462
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   792 AA;  89764 MW;  9B66040B7B1BD3EA CRC64;
     MLTDSRSLCF PEETLFFALK TQRNDGHRYI QDLYNRGVRQ FVVEQVPEAY ETLYPQANFL
     RVPHTLAALQ RLAERHRDEF SLPIVGITGS NGKTMVKEWL YQLLLPSQRI VRSPRSYNSQ
     IGVPLSVWLL NEQTEVGIFE AGISQPGEMM ALRDIIQPTI GVLTSLGAAH QENFRSMEEK
     CMEKLELMHD TEAMVYCSDN DIVSRCIRRM NYKGEKISWS TCDQQAAFYV KSVENSHITY
     IWKEEENCFD IPFIDEASIE DCITCAAVAL RLGLTPGDLA DRMPKLEPVA MRLEVKEGQR
     GCILINDSYN SDINSLDIAL DFMNRREELK KRTLILSDMF QSGLSPEKLY AQVSELAVKR
     GITKFIGIGA QLTAQADKIQ IADKQFFADV NHFLGSDAFT GLRNEMILLK GARPFGFDQI
     TEQLEQKVHE TILEVNLNAV VENLNYYRSF MKPETKMVCM IKADAYGAGA VEIAKTLQDH
     RVDYLAVAVA DEGVTLRKAG ITANIMIMNP EMTAFKTMFD YDLEPEVYSF RLLDALIKAA
     RKEGITGWPV HIKLDTGMHR LGFDPEQDMD ELIDRLTHQQ AVIPRSVFSH FVGSDSDDFD
     NFSTLQFKRF EMGSQKLQAA FSHKILRHID NSAGIEHFPD RQLDMCRLGL GLYGIDSRDN
     RILHTVSTLK TTILQMHQVP KSETVGYSRK GKLTRDSVIA AIPIGYADGL NRRLGNRHCY
     CLVNGQKAEY VGNICMDVAL IDVTDIPCQE GDQVEIFGEH LPVTVLSDVL ETIPYEVLTG
     ISNRVKRVYF QD
//
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