ID A0A374TFF5_9BACT Unreviewed; 825 AA.
AC A0A374TFF5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=DXD25_00770 {ECO:0000313|EMBL:RGK35947.1};
OS Prevotella sp. TF12-30.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2292365 {ECO:0000313|EMBL:RGK35947.1, ECO:0000313|Proteomes:UP000262185};
RN [1] {ECO:0000313|EMBL:RGK35947.1, ECO:0000313|Proteomes:UP000262185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF12-30 {ECO:0000313|EMBL:RGK35947.1,
RC ECO:0000313|Proteomes:UP000262185};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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:RGK35947.1}.
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DR EMBL; QSQJ01000001; RGK35947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A374TFF5; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000262185; 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; 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:RGK35947.1};
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 495
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 593
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 495
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 825 AA; 92902 MW; 22F597202249FF72 CRC64;
MTYTIEKVTT LIGARRYGDN DTNIGFILTD SRSLCFPEET LFFALKSERN DGHNYIPELY
RRGVKNFVVT DVPKGYASDY PEANFLKVVN TLEALQRLAE RHRDEFNIPI VGITGSNGKT
MVKEWLYQLL SPSMFVTRSP RSYNSQIGVP LSVWLMNEQT QVGVFEAGIS QPGEMLALRD
IIQPTIAVLT NVGSAHQENF SSLEEKCREK LILFHDAETV VYDGDDEVIT KVVAEYPDYK
GEKLFWSLKN PEAPFYVKKI EKQQSVSVIT YIYKGVEDSF SIPFIDDASI QNSIICAAVA
SKIGLSAEDI DKRMALLEPV AMRLEVKVGQ HGCTLINDSY NSDINSLDIA LDFMNRRPDH
RGRRHTLILS DIYQSGQTPE ALYKEVSDLA RKRGVVKFIG IGPELCKQHD TIQISEKFFF
PNVEEFINSE VFASLRDEVI LLKGARQFGF DQLTELLVQK VHETTLEVNL NAVVANLNYY
RAFMKPETKL VCMIKADGYG AGAVEIAKTL QDHRVDYLAV AVADEGVTLR KNGITSNIMI
MNPEMTAFKT MFDYDLEPEV YSFRLLDALI KAAEKEGVTG FPVHIKLDTG MHRMGFDPEN
DMEELIGKLK HQNAIIPRSV FSHFVGSDDD SFDDFSAHQF ELFDKGSRQL QAAFDHKILR
HICNSAGIEH FPERQLDMCR LGLGLYGINS RNNKTINCVS TLKTTILQMH NVKAGDSVGY
SRKTILDKDS VIAAIPIGYA DGLNRRLGNR HAYCLVNGQK ADYVGNICMD VAMIDVTGIN
CKEGDSVEIF GEHLPVQVLS DILETIPYEV LTTISNRVKR VYYQD
//
