ID A0A090VX26_9FLAO Unreviewed; 370 AA.
AC A0A090VX26;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=JCM19301_3711 {ECO:0000313|EMBL:GAL65251.1}, JCM19302_4034
GN {ECO:0000313|EMBL:GAL69305.1}, JCM19538_2148
GN {ECO:0000313|EMBL:GAL89159.1};
OS Jejuia pallidilutea.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Jejuia.
OX NCBI_TaxID=504487 {ECO:0000313|EMBL:GAL69305.1, ECO:0000313|Proteomes:UP000029646};
RN [1] {ECO:0000313|Proteomes:UP000029641, ECO:0000313|Proteomes:UP000029646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19301 {ECO:0000313|EMBL:GAL65251.1,
RC ECO:0000313|Proteomes:UP000029641}, JCM 19302
RC {ECO:0000313|EMBL:GAL69305.1}, JCM 19538 {ECO:0000313|EMBL:GAL89159.1,
RC ECO:0000313|Proteomes:UP000030184}, and JCM19302
RC {ECO:0000313|Proteomes:UP000029646};
RA Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K.,
RA Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., Niwa A.,
RA Sawabe T., Sawabe T.;
RT "Draft Genome Sequence of Marine Flavobacterium Jejuia pallidilutea Strain
RT 11shimoA1 and Pigmentation Mutants.";
RL Genome Announc. 2:e01236-14(2014).
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:GAL69305.1}.
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DR EMBL; BBNR01000001; GAL65251.1; -; Genomic_DNA.
DR EMBL; BBNS01000001; GAL69305.1; -; Genomic_DNA.
DR EMBL; BBNY01000005; GAL89159.1; -; Genomic_DNA.
DR RefSeq; WP_042240033.1; NZ_BBNY01000005.1.
DR AlphaFoldDB; A0A090VX26; -.
DR STRING; 504487.JCM19538_2148; -.
DR eggNOG; COG0787; Bacteria.
DR OrthoDB; 9801978at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000029641; Unassembled WGS sequence.
DR Proteomes; UP000029646; Unassembled WGS sequence.
DR Proteomes; UP000030184; 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}.
FT DOMAIN 243..369
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 38
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 264
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 38
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 370 AA; 40754 MW; A6E2185C0AC42090 CRC64;
MPKVQETILE IDLKALKHNF EYLKSKLKNG TQFLAVVKAF AYGNDAEEIA TYLQNLNIDY
FAVAYANEGA ALRKAGVTKP ILVLHTLAVN FDVILENCLE PSLYNAKILS EFIDFAENEN
QKAYPIHIKF NTGLNRLGFS ESDSGYIVEK IKTTQSIKVK SLFSHLAASE DLNEKVFTLN
QIHSFKSIAN NFSKAIGYQP ILHMSNTSGV LNYPEAHLDM VRCGIGLYGF GNSKKESANL
KPIASLKTVI SQIHHIKKGA SVGYNRAFKN KDTLIKTATL PLGHADGISR IYGNNKGFVT
INGKKAPIIG NVCMDMIMVN ITHIDCKEGD EVTVFDGKTT TAEVLAEGAG TISYELITGI
SQRVKRVVLK
//
