ID A0A2V1IWF8_9BACT Unreviewed; 825 AA.
AC A0A2V1IWF8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN ORFNames=C5O25_06215 {ECO:0000313|EMBL:PWB07727.1};
OS Paramuribaculum intestinale.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae;
OC Paramuribaculum.
OX NCBI_TaxID=2094151 {ECO:0000313|EMBL:PWB07727.1, ECO:0000313|Proteomes:UP000244925};
RN [1] {ECO:0000313|Proteomes:UP000244925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100764 {ECO:0000313|Proteomes:UP000244925};
RA Clavel T., Strowig T.;
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWB07727.1}.
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DR EMBL; PUBV01000010; PWB07727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1IWF8; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000244925; Unassembled WGS sequence.
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; 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; 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:PWB07727.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}.
FT DOMAIN 699..823
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 493
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 720
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 591
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 769
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 493
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 825 AA; 92259 MW; C29BA8B7E95CD72D CRC64;
MNYKISRIAE TIHASLPSPA DPDHEISILL TDSRSLTYPD QSIFFAIRTR NNDGHRYMRD
LYDRGVRHFV ARHIPDDMAS ATDAVILLVP SVTRALQDLA RAHRSRFDIP VVGITGSRGK
TTVKEWLYQL LSSDYSIVRS PRSYNSQIGV PLSIWELDTD TTMAIFEAGI SLPDEMTALQ
GIIKPNIGII TNIGPEHADG FTSLRTKCDE KVILMRDCDV IIYNGDDRVI SEAVSEACIP
AKEIAWSTRD SDRPLFISAI RRHRETTDID FSYLRTDGSV TIPFTSDADI QNAIHCLALM
LYLNRPADIT ASRISQLAPV ATRMEVKEGV NDCLVIYDAY TSDLNSLQPA LDFLNRRRTG
RRSVTAIISD VMHETLEPQR LYREVARLLT QRGVDRVIGV GEEISANSRY FPADSRFFPS
TSVMLSEMSA DDFDRELVLV KGASRFHFEM IAEMLEARQH ETVLEVNLDA LVSNFNLYRS
MLRPTTGIIC MVKASGYGAG SYELAKTLQA QGAAYMAVAV LDEGVELREA GITMPVMVMN
PHVANYKTMF AYRLEPEVYS FGILREIIRE GEKCGITDFP VHIKLDTGMH RLGFIPEEIP
ELIDLLRRQK VVRPHSLFSH LATADCPHLN SYTEGQLKLF DSMCAQIQSA FSHYIMRHIL
NSAGIARYPS HQYDMVRLGI GLYGVATLPG GEPAGLRTVS SLRTVIISIR EWPAGTTIGY
GCRGVCTRRS RIATIPVGYA DGIDRHLGNG GMRVWINGHR CPSIGNICMD ACMIDVTDAD
CQVGDRVEIF GDNVPVEDLS DVLDTIPYEM LTSVSTRVKR IYYRE
//
