ID A0A1M4YNF0_9FLAO Unreviewed; 815 AA.
AC A0A1M4YNF0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=SAMN05444408_108126 {ECO:0000313|EMBL:SHF07183.1};
OS Chryseobacterium takakiae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1302685 {ECO:0000313|EMBL:SHF07183.1, ECO:0000313|Proteomes:UP000184236};
RN [1] {ECO:0000313|EMBL:SHF07183.1, ECO:0000313|Proteomes:UP000184236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26898 {ECO:0000313|EMBL:SHF07183.1,
RC ECO:0000313|Proteomes:UP000184236};
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; FQVO01000008; SHF07183.1; -; Genomic_DNA.
DR RefSeq; WP_072884979.1; NZ_FQVO01000008.1.
DR AlphaFoldDB; A0A1M4YNF0; -.
DR STRING; 1302685.SAMN05444408_108126; -.
DR OrthoDB; 9801978at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000184236; 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 Ligase {ECO:0000313|EMBL:SHF07183.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}.
FT DOMAIN 688..813
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 815 AA; 92912 MW; 59620CBB1FA5AFAF CRC64;
MNYTVHQIAE IANAHVIGDG KLLIKNIAFD SRIIYSTKNT AFIAINTHKN SGEKFIEAAI
DRGIQVIISE NHYPNYENIT WIITENAVVF LQKLAKYHFE NAYIKSIGIT GSNGKTILKE
WLYQCLWNEF TTVKSPKSFN SQIGLPLSLL QINDSHELGI FEVGISKPDE MEKQENIFHP
QIGLLTHIGT AHLANFTFEE QLVDEKIKLF RNSKVIIYNG DNILVDSKIK ELYSTKRLIT
YGFKEHNDVH FKNNLSREED VVVQYFNEQI SFPVNQRDEA TLINALALLT VLKELEISND
KIIEKINALK AVEMRLEAIE GIKNNIVIND SFNLDLDSLK TALQFLNEYN KPKKSLVLTD
IVGVNSNSRE LYEEVSELVN EQRFDSVFLI GNEISNYSEL FKSKTSTYIN TRELIDSKHL
TEIENQIILL KGARKFEIEK LKDILELRKH DTVLEINLNA ILHNINYHKS LLKPATKMMA
MVKANAYGLG SYEISEFLQH HHIDYLGVAF VDEGVELRKK GITVPIVVMN PEQHSYDTVI
AYNLEPEIYS LRVLEQFYEA VKKSGYDKKY PIHIKLETGM HRLGFKDSEL DELSRTLAEK
NLKVQSIFSH LSSSDLPSEK EFTLHQLNTF ERNSNYLIEN LGYTPIRHIL NSSGITNYTD
HQYDMVRIGI GMLGESQNSE INKQLRSVVS FKTVISQISI VGDGESVGYS RRFKTDHPTK
IATIPVGYAD GIPRLIGNQV GNVGIHKTLA PIVGNICMDM MMINVDHISN VKEGDTVTVF
NAKPTLKEFA DYCKTITYEV LTSISPRVKR IYVKD
//
