ID J9R4F5_RIEAN Unreviewed; 814 AA.
AC J9R4F5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
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=B739_0721 {ECO:0000313|EMBL:AFR35323.1};
OS Riemerella anatipestifer RA-CH-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Riemerella.
OX NCBI_TaxID=1228997 {ECO:0000313|EMBL:AFR35323.1, ECO:0000313|Proteomes:UP000006276};
RN [1] {ECO:0000313|EMBL:AFR35323.1, ECO:0000313|Proteomes:UP000006276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA-CH-1 {ECO:0000313|EMBL:AFR35323.1,
RC ECO:0000313|Proteomes:UP000006276};
RA Chun C.A., Shu W.M., Kang Z.D., Jia W.X.;
RT "Riemerella anatipestifer vaccine strains.";
RL Submitted (SEP-2012) 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; CP003787; AFR35323.1; -; Genomic_DNA.
DR RefSeq; WP_014937731.1; NC_018609.1.
DR AlphaFoldDB; J9R4F5; -.
DR STRING; 34085.AB406_1055; -.
DR KEGG; rag:B739_0721; -.
DR PATRIC; fig|1228997.3.peg.717; -.
DR HOGENOM; CLU_372082_0_0_10; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000006276; Chromosome.
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; 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 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000006276}.
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 582
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; 92567 MW; 8CC385AF5DC5A773 CRC64;
MNYTARQIAE ITGAKLIGAG DKIIKHFAFD SRIIYSPKNT GFVAIKTKKN NGEKYIASAV
EKGIELIVSE HKTLDNEHLS WLIVDDTVKF LQKLAHLHLK SHNIQTIGIT GSNGKTIIKE
WLYQCLSEDI RCVKSPKSFN SQIGLPLSLL NIRPEHKVGI FEVGISEPNE MEVLETIFSP
KIGVLTHIGS AHISNFKSEE HLIDEKISLF KDSENIIFNG DNTLVNNKIN TLYSSKNLIS
YGFNKDNNIH ISSNWKDRQQ PITVQCFDKS FSFPAQQRDE ATLSNVLAII AVMHLLGFST
EKMIEKINNL KAVEMRLESV NGIKNNLIIN DSFNLDLDSL KIAFEFIKSY QKPKKSLIIT
DFTEKSDADN LYQEVASLIN EQNFNKVFLI GEEISQYQHL LNTESFSFNT TNDLFSNQEF
KDLENELILL KGARKFEIEQ VKTYLELQKH DTVLEVNLNN LLHNINVHRS LLKPETKIMA
MVKAYSYGLG GYEIAEFLQH HHIDYLGVAV ADEGVELRKN GITVPIVVMN PEQHSYNTII
EYNLEPNIYS FRVLELFHKQ LKQNGYEGRY PIHIKLETGM HRLGFKEDEI DQLKDYLNQM
SVKVESIFSH LSSSDIPQEK DYTLAQCQKF DRLSQNIIKD LNYKPLRHIL NSAGITNYTD
YQMDMVRIGI GMMGISASPE IQPLLNPVVA FKSVISQISE IQPNDSVSYG RRYKASKSTR
IATIPVGYAD GVPRLLSNGV GYIGIKNTLC PIVGSVCMDM MMVDISDLPA KEGDEVIIFY
EKPSLEDFAM YSQTIPYEVL TSISRRVKRV YIKD
//
