ID A0A1G6K8U9_9BACT Unreviewed; 372 AA.
AC A0A1G6K8U9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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:TGG88466.1};
GN ORFNames=E4650_05325 {ECO:0000313|EMBL:TGG88466.1}, SAMN04488588_0784
GN {ECO:0000313|EMBL:SDC27492.1};
OS Geotoga petraea.
OC Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae; Geotoga.
OX NCBI_TaxID=28234 {ECO:0000313|EMBL:SDC27492.1, ECO:0000313|Proteomes:UP000199322};
RN [1] {ECO:0000313|EMBL:SDC27492.1, ECO:0000313|Proteomes:UP000199322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WG14 {ECO:0000313|EMBL:SDC27492.1,
RC ECO:0000313|Proteomes:UP000199322};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TGG88466.1, ECO:0000313|Proteomes:UP000297288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO-Geo1 {ECO:0000313|EMBL:TGG88466.1,
RC ECO:0000313|Proteomes:UP000297288};
RA Grouzdev D.S., Semenova E.M., Sokolova D.S., Tourova T.P., Poltaraus A.B.,
RA Nazina T.N.;
RT "Draft genome sequence data and analysis of a Fermenting Bacterium, Geotoga
RT petraea strain HO-Geo1, isolated from heavy-oil petroleum reservoir in
RT Russia.";
RL Submitted (APR-2019) 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; FMYV01000002; SDC27492.1; -; Genomic_DNA.
DR EMBL; SRME01000002; TGG88466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6K8U9; -.
DR STRING; 28234.SAMN04488588_0784; -.
DR OrthoDB; 9813814at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000199322; Unassembled WGS sequence.
DR Proteomes; UP000297288; Unassembled WGS sequence.
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; 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.
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:UP000199322}.
FT DOMAIN 242..365
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 37
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 263
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 37
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 372 AA; 42473 MW; 1602B683F8CBBC70 CRC64;
MLKNSRSTYA EINIDNYLHN LEYISKKTNT EVMPVLKADA YGHNKITLAK CAVKEGYKRF
AVAFLEEALD LINNDIKKPI LIFNYINPKS LKRYTYFSDF LIPTIHSLNN LKTLISELGE
EINKFKFHLN FNTGINRIGI QENEIENIIA IIKNKNINIE GIYSHYATAD SLDDYVDYQY
NNFLRIIKIF KDREIEYKFK HMSNSAACLY YPERSLDIVR PGIASFGLQP SNIKKDENIK
PVMELKSIVA KINTCKKGDT IGYGRTHIID KNSKTAIIPI GYADGYPRIL SNKSHVLIKN
KLYKVIGNVS MDQIVIEIKD DDIMVGDEVI LFGKKPSAEH LANLANTLNY EITCGVSSRV
PRVFIKGGSY FE
//
