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Database: UniProt
Entry: A0A1M7FCY9_9FLAO
LinkDB: A0A1M7FCY9_9FLAO
Original site: A0A1M7FCY9_9FLAO 
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
//
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