ID ALR2_RHILO Reviewed; 381 AA.
AC Q98F05;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Alanine racemase, catabolic;
DE EC=5.1.1.1;
GN Name=dadB; OrderedLocusNames=mll3997;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
CC -!- FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized to
CC pyruvate by DadA. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}.
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DR EMBL; BA000012; BAB50762.1; -; Genomic_DNA.
DR RefSeq; WP_010912105.1; NC_002678.2.
DR AlphaFoldDB; Q98F05; -.
DR SMR; Q98F05; -.
DR KEGG; mlo:mll3997; -.
DR PATRIC; fig|266835.9.peg.3173; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_1_1_5; -.
DR Proteomes; UP000000552; 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:0006522; P:alanine metabolic process; IEA:UniProtKB-UniRule.
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; Pyridoxal phosphate.
FT CHAIN 1..381
FT /note="Alanine racemase, catabolic"
FT /id="PRO_0000114552"
FT ACT_SITE 55
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000250"
FT ACT_SITE 276
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 381 AA; 39784 MW; 22B0C7837380066F CRC64;
MNDAVNPTAA KTVTGWPVSE AAAGAILTID LGAIRENYRR LKALLGGVHC AGVVKANGYG
LGAAKVAAAL TREGCDIFFV ALLAEGIALR KAVGTGPDIY VLNGLPPGSE PEAVAAGLCA
VINSGAQLKA WRAAVHDAGR RLPAAIQVDS GMSRLGMAPA EVEALAGDSS AFDGIDIKYV
MSHLACADEP RHPANEQQRL AFERLRAMLP RAPASLANSS GIFLGPSYHH DLARPGAALY
GINPTPGEPN PMLPVVWLQA KVAQTRRIEK GAGIGYGHSY HADGPLSLAT ISFGYADGWL
RRSASAAWFE GVRLPFLGRV SMDSIILDIS ALPPGRLREG DLVELLGPSQ SVDDAAGHAG
TIGYEILASL GPRFHRHYVG G
//
