ID A0A1M7FCY9_9FLAO Unreviewed; 816 AA.
AC A0A1M7FCY9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN05216269_102116 {ECO:0000313|EMBL:SHM01843.1};
OS Flavobacterium xinjiangense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=178356 {ECO:0000313|EMBL:SHM01843.1, ECO:0000313|Proteomes:UP000184092};
RN [1] {ECO:0000313|EMBL:SHM01843.1, ECO:0000313|Proteomes:UP000184092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.2749 {ECO:0000313|EMBL:SHM01843.1,
RC ECO:0000313|Proteomes:UP000184092};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRCL01000002; SHM01843.1; -; Genomic_DNA.
DR RefSeq; WP_073205119.1; NZ_FRCL01000002.1.
DR AlphaFoldDB; A0A1M7FCY9; -.
DR STRING; 178356.SAMN05216269_102116; -.
DR OrthoDB; 9801978at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000184092; Unassembled WGS sequence.
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}.
FT DOMAIN 690..814
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 485
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 711
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 583
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 760
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 485
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 816 AA; 91281 MW; C003168778831B5F CRC64;
MILKIQNIIS QMQAVFVDSN KIKTIDAVSI DSRSLQNGSQ TLFFALVGAN NDAHLYIENL
IEKGVQNFVV THIPVDCAGK ANFLIVENTL EALQQFASFY RSLFDFPVIG LTGSNGKTIV
KEWLNFLLSP DYNAIRSPKS YNSQVGVPLS VLAINEQHNL GIFEAGISTG SEMGKLEKII
KPTIGILTNI GSAHDEGFGS LGEKISEKLL LFKDSEVLIY QKSEIVDANL FRYENRRLFS
WSFKDSTADV FITKSPVLDQ TILHIRHVEE SFEIQIPFQD AASVENAISC LMVLLYFKYD
VTTIQNRMKL LYPVEMRLKV KNGINNCSVV DDSYSSDFQS LKIALDFLES QKQYQKKTVI
LSDIFQSGLS NEELYSKVAE LIISNRISRV IGIGETISAF KDKFTNCITY KNTADFIADF
DDLIFSNETI LIKGARTFQF EEIVSLLEEK THETVLEINL NAISHNLNFF KSKLKPATKM
MVMVKAFGYG NGGFEIAKLL EHHKVDYLGV AFADEGISLK NLGIQLPIMV LNPESTSFSA
IIQHQLEPEI YSLKGLRAFL KIAEQKKLKN FPIHIKLDTG MHRLGFEANT IDDLIETLRG
NKTVEIKSIL SHMATSDDEN HKDFAESQIN LFEKLSSKLM VELQIKPIRH ILNTSGISNF
PASQFDMVRL GIGLYGISND AEEQKYLENV GTLKSIISQI RTIPAGDSVG YGRRFVAEKP
TKVATIPIGY ADGISRAWGN GNGYIAIKDK KASIIGSVCM DMLMIDITGV ACNEGDTVVI
FGENPTVNYL AEKLNTIPYE ILTSVSQRVK RVFYRE
//