ID A0A0G3WFG0_9BACT Unreviewed; 391 AA.
AC A0A0G3WFG0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN Name=alr {ECO:0000313|EMBL:AKL97396.1};
GN ORFNames=Epro_0017 {ECO:0000313|EMBL:AKL97396.1};
OS Endomicrobium proavitum.
OC Bacteria; Elusimicrobiota; Endomicrobiia; Endomicrobiales;
OC Endomicrobiaceae; Endomicrobium.
OX NCBI_TaxID=1408281 {ECO:0000313|EMBL:AKL97396.1, ECO:0000313|Proteomes:UP000035337};
RN [1] {ECO:0000313|EMBL:AKL97396.1, ECO:0000313|Proteomes:UP000035337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rsa215 {ECO:0000313|EMBL:AKL97396.1,
RC ECO:0000313|Proteomes:UP000035337};
RA Zheng H.;
RT "Complete genome sequence of Endomicrobium proavitum.";
RL Submitted (SEP-2014) 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}.
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DR EMBL; CP009498; AKL97396.1; -; Genomic_DNA.
DR RefSeq; WP_052569488.1; NZ_CP009498.1.
DR AlphaFoldDB; A0A0G3WFG0; -.
DR STRING; 1408281.Epro_0017; -.
DR KEGG; epo:Epro_0017; -.
DR PATRIC; fig|1408281.3.peg.17; -.
DR OrthoDB; 9813814at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000035337; 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:UP000035337}.
FT DOMAIN 263..391
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 57
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 284
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 57
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 391 AA; 43312 MW; 2777BB254C217DCC CRC64;
MKKEPPPALT NLFFPKKRTP VFFRQNWVEV DKSDFHFNLK KIKEHLAKDT KIMTVIKANA
YGHGGVALAK EAQKAGISWI AVSSLEEGIT FREAGIKTNI LVLGGLYPFE NLQVAIVHNL
TPTISTMAAL SALEDMAVRH NKIANFHLAV DTGMGRIGSL SESVYPMLQK IAQTPELNMT
GMYTHFTVAD TDPVFTQMQL ESFTKIVKYA RQTLGLKFIA HSANSAALFR NKRTHLDMVR
PGISLFGLSP FKHAERFIKL KPVLTWKTKI SFLKRVPSGF CVSYGRTFVT TKESVIATIP
VGYADGYNRL LSNKGDVLVR GKRCPIAGRI TMDMTMIDVT GVKGVALGDE VVLIGAQGKE
QIKVDELAKI QDTINYEVTC AISPRVPRIV V
//
