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Database: UniProt/TrEMBL
Entry: A0A0M4HQ12_9BACT
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ID   A0A0M4HQ12_9BACT        Unreviewed;       832 AA.
AC   A0A0M4HQ12;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=AM218_12610 {ECO:0000313|EMBL:ALD21892.1};
OS   Hymenobacter sp. DG25A.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1385663 {ECO:0000313|EMBL:ALD21892.1};
RN   [1] {ECO:0000313|EMBL:ALD21892.1, ECO:0000313|Proteomes:UP000061697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG25A {ECO:0000313|EMBL:ALD21892.1,
RC   ECO:0000313|Proteomes:UP000061697};
RA   Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA   Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA   Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA   Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA   Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA   Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA   Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA   Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA   Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL   Submitted (AUG-2015) 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; CP012623; ALD21892.1; -; Genomic_DNA.
DR   RefSeq; WP_054414174.1; NZ_CP012623.1.
DR   AlphaFoldDB; A0A0M4HQ12; -.
DR   STRING; 1385663.AM218_12610; -.
DR   KEGG; hye:AM218_12610; -.
DR   PATRIC; fig|1385663.3.peg.2593; -.
DR   OrthoDB; 9801978at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000061697; 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; IPR000713; Mur_ligase_N.
DR   InterPro; IPR035911; MurE/MurF_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   NCBIfam; TIGR00492; alr; 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; PF01225; Mur_ligase; 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          704..830
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        500
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        725
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         596
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         775
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         500
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   832 AA;  92047 MW;  CFCFA6B10919AFE5 CRC64;
     MLLFSHLPDI TGGTLLPTPA ALHRPVQHLL LDSRHVGVAA GALFFAIRGA QHNGHRYLPD
     LYQQGVRQFV VDRAEEIPQG LEAYPEACFL LVADSLLALQ TVAAHHRLQF HVPVVGITGS
     NGKTIVKEWL AQMLSPDELI CKSPRSYNSQ VGVPLSVWEL NSTHTFGIFE AGISERGEME
     RLARVIQPTL GIFTNLGTAH DAGFTSATEK AREKMRLFAG VDTLFYCRDH ALVHAIAQEV
     LDESRTFTWS RQHPQQAHVA VTVAEASADR TVVHVALDRP LPQEYTFTVP FADEPSLENA
     LHVLTVLLWL QVPATEIQHR LDRLHPVAMR LEMKQALNDC YILDDTYNND LAGLSLALDM
     LARQPRRGRR SLILSDLLES GLPAAELYAR VATQLATHGV ERLLGVGPDI SAHAEVFQDI
     DKEFFADTEA FLTQVRPEQF RHETILVKGA RRFGFERIVS AFQQKIHGTV LEVNFDALVH
     NLNFYRTRLQ PGTKLMVMVK AFAYGSGSYE VANLLQFHRA DYLAVAYTDE GVELREQGIS
     LPLMVMNPSP DSFQKMHQYH LEPEIYSFEV LQQYLAVAAE QPLPAIHLKL DTGMRRLGFA
     EEDMPQLCAL LRANADRLRV ASALTHLAGA DEEQHNSFSQ QQLAAFSRMT PLVEAALGYS
     IIKHALNSAG ILRFPQAHFD MVRLGIGLYG VEATGQEQEA LRPVSTLRTT VSQVKTLAAG
     QTVGYGRRGS ATAHDRRIAT LAIGYADGYD RRFGNGGGEV VIRGQRAPIV GNVCMDMCMA
     DVTHITGAQA GDTAEVFGPG ITLSELATRI GTIPYELLTN VSERVKRVFF AE
//
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