ID A0A1I0WX83_9FLAO Unreviewed; 814 AA.
AC A0A1I0WX83;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN05660845_1056 {ECO:0000313|EMBL:SFA93325.1};
OS Flavobacterium swingsii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=498292 {ECO:0000313|EMBL:SFA93325.1, ECO:0000313|Proteomes:UP000199604};
RN [1] {ECO:0000313|EMBL:SFA93325.1, ECO:0000313|Proteomes:UP000199604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21789 {ECO:0000313|EMBL:SFA93325.1,
RC ECO:0000313|Proteomes:UP000199604};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOJT01000002; SFA93325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0WX83; -.
DR STRING; 498292.SAMN05660845_1056; -.
DR OrthoDB; 9801978at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000199604; Unassembled WGS sequence.
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:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
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 InterPro; IPR005863; UDP-N-AcMur_synth.
DR NCBIfam; TIGR00492; alr; 1.
DR NCBIfam; TIGR01143; murF; 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:SFA93325.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}.
FT DOMAIN 688..812
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 483
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 709
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 581
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 758
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 483
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 814 AA; 92138 MW; F84AD2331465B9BC CRC64;
MAISLHNIIP VLNADFQGIE TDIHINNISI DSRSLQNNEN TLFFAIVGPN NDAHIYIGDL
ISKGVKNFVV TYIPQRLKDK ANFLIVENTL FALQKFASYY RNLFHFPVIG ITGSNGKTIV
KEWLNFLLSP DYNIIRSPKS YNSQVGVPLS VIGINEHHNF GIFEAGISTK GEMENLQKII
QPSIGILTNI GTAHDEGFAD ISEKIKEKLK LFTNVEVLIL NKNKTIEAFI KSEIKTFTWS
TNDKSADVFF QKKTFDDYSI LNITNEEKCF KIQIPFTDEA SLENSMHCIL TMLYLKYDLD
TIEHRVSQLF PVEMRLKVKK GINNCTLIDD SYSADFQSLK IALDFLENQK QHLKKTLILS
DIYQSGLEDE NLYARVSQLI ISNKINRVIC IGDIISKYKN KFLNAISYVS TNDFIDDFEN
LDFANETILI KGSRHFEFEK IVTLLEEKTH ETVLEINLNA ISHNLNYYKS KLNPETKIMV
MVKAFGYGSG GFEIAKLLAH HKVDYLGVAF ADEGIELRQA GIELPIMVLN PEMTSFPSII
QYNLEPEIYS IRGLKAFIKI TEQKELTNYP IHIKINTGMN RLGFDDEIIP ELISILQKND
SIQVKSILSH LAASDDLTHD IFTKKQISDF DIISSKITRE LKIYPIRHIS NTSAISNYPQ
AQFDMVRLGI GLYGVSNDIN ETEELENVGT LKSIISQIRT LDIGESVGYS RRFMVEKPTK
TATIPIGYAD GISRSWGNGV GYVLINEQKA PIIGSICMDM LMVDVTEINC FEGNEVVIFG
KNPSVTTIAK AINTIPYEIL TSISGRVKRV FYRE
//
