ID A0A2U2XBV7_9FLAO Unreviewed; 760 AA.
AC A0A2U2XBV7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN Name=alr {ECO:0000313|EMBL:PWH85289.1};
GN ORFNames=DIT68_10140 {ECO:0000313|EMBL:PWH85289.1};
OS Brumimicrobium oceani.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Crocinitomicaceae; Brumimicrobium.
OX NCBI_TaxID=2100725 {ECO:0000313|EMBL:PWH85289.1, ECO:0000313|Proteomes:UP000245370};
RN [1] {ECO:0000313|EMBL:PWH85289.1, ECO:0000313|Proteomes:UP000245370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C305 {ECO:0000313|EMBL:PWH85289.1,
RC ECO:0000313|Proteomes:UP000245370};
RA Kou Y.;
RT "Brumimicrobium oceani sp. nov., isolated from coastal sediment.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWH85289.1, ECO:0000313|Proteomes:UP000245370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C305 {ECO:0000313|EMBL:PWH85289.1,
RC ECO:0000313|Proteomes:UP000245370};
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Rusch D., Podicherti R., Tsui H.-C.T.,
RA Winkler M.E.;
RL Submitted (MAY-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWH85289.1}.
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DR EMBL; QFRJ01000007; PWH85289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2XBV7; -.
DR OrthoDB; 9801978at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000245370; 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}; Reference proteome {ECO:0000313|Proteomes:UP000245370}.
FT DOMAIN 635..759
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 430
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 656
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 528
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 705
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 430
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 760 AA; 86106 MW; 1FE90C04C96A4D97 CRC64;
MNLNLSHKEL ITIISGESSS FPEYPIDIIY YDTRLINTSR NGVFFALNGR RNGHDFINKA
YEKGIRTFVV NKTVDLPADA TIITVEDPLR ALQAVAKHHR NQFSYPVLAI TGSLGKTTIK
EWLYFLLSDE FNIVRSPKSF NSQIGVAISL LEMNDQHNLA IIEADISHPN EMEFIEDMVS
PTLGIYTGVG HFYADNFESQ KAHAAEHLKL FKHANITFVL SEHKNELRKN KINSDIVDYD
AWKKLDFSQL SYSNNRVIAL HVAEFLGVEK SILFKKGEQL PVLSNRMEVF EGQDDNLIIN
DSYNIDVDAL EQALSYQFSS DERKDKIVVL DLSYVEENRK KDILNVVNSY SPTQLFIIEN
NEVPAELLAV KNSSILFKGS YRSRLKETVL MFKNRKHETW VEFDLKSIQH NISVFQKKLP
EKTKLLVMVK ASSYGTGDIN IPHFLQQTGI DYLGVAYTDE GTTLRENGIS LPILIMNTEI
DAFDDVIRFQ LEPSIFSIAQ LEAFCNRLRE DNISDFPIHI TVETGMNRLG FYPEDIAELI
EKLKLRPEVK VKSIYSHLAD ADNADPAYSL EQIEKFKAMK TTFKNGLQDD EILYHILNSE
GASKFGKFAS FDMVRLGIGV FGYTSTAAED ELLPSIRWKT TISQIKTIQA GETVGYSRTF
TAEKPMEIAT LRIGYADGFR RSLSNGVGQV FINGISCPVV GNVCMDMTMV DVSNTNCQAG
DEVEIIGENI PIKTFSNRLK TIPYEVMTSI SKRVSRIYLR
//
