ID A0A259URH5_9FIRM Unreviewed; 736 AA.
AC A0A259URH5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=D-ornithine 4,5-aminomutase subunit beta {ECO:0000313|EMBL:OZC20721.1};
DE EC=5.4.3.5 {ECO:0000313|EMBL:OZC20721.1};
GN Name=oraE {ECO:0000313|EMBL:OZC20721.1};
GN ORFNames=SPSIL_15890 {ECO:0000313|EMBL:OZC20721.1};
OS Sporomusa silvacetica DSM 10669.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=1123289 {ECO:0000313|EMBL:OZC20721.1, ECO:0000313|Proteomes:UP000216752};
RN [1] {ECO:0000313|EMBL:OZC20721.1, ECO:0000313|Proteomes:UP000216752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10669 {ECO:0000313|EMBL:OZC20721.1,
RC ECO:0000313|Proteomes:UP000216752};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Sporomusa silvacetica DSM 10669.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
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:OZC20721.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LSLK01000059; OZC20721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259URH5; -.
DR OrthoDB; 9759220at2; -.
DR Proteomes; UP000216752; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0047831; F:D-ornithine 4,5-aminomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 3.20.20.440; D-Lysine 5,6-aminomutase alpha subunit; 1.
DR Gene3D; 3.30.30.60; D-lysine 5,6-aminomutase beta subunit KamE, N-terminal domain; 1.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR028991; KamE_N.
DR InterPro; IPR036843; KamE_N_sf.
DR InterPro; IPR015130; Lys-AminoMut_A.
DR InterPro; IPR037086; Lys-AminoMut_asu_sf.
DR NCBIfam; NF040743; ornith_mutase_E; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF09043; Lys-AminoMut_A; 1.
DR Pfam; PF16554; OAM_dimer; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 4: Predicted;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:OZC20721.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216752}.
FT DOMAIN 594..732
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 736 AA; 81079 MW; 8AB3742EC459FE00 CRC64;
MTLEVDEKLN LNNLLTDLQS YRPRRKGWTW RSRPGTRELG PFTYNQVSEP LKQSCPLPAA
KYFNSIDPQP DCVITTEIAS GRFEDDIRRM RMAAWHGADH IMVIRTAGQS HFDGLIEGTP
EGVGGVPITR KQLRATRKAL DWIEDEVGRP INFHSYVSGV AGPEVAVLLA EEGVNGAHQD
PQYNVLYRNV NMHRSFVDAA VAKQIMAAAG MAQIDGAHNA NATAREAWKV MPELMVQHAI
NCQYSIMVGM PKDKICLSTV PPTSPPAPCI SLDLPYAVAL RQLFEGFRFR AQMNTKYMES
CTREVTVTHV LNALLSRLTS ADIQSTITPD EGRNVPWHYN NIHGVNTAKQ ALLGLDGLLN
MVSLNFDGEL GVKVRELKER ACLFMEEIIA AGGYFSAVSQ SFFVDSGMYP ERNGDGIARQ
INGGVGVGTI VPRDIDYMAP VCDHFGYNAL PAGVTKACEL IGDCTLCSPD KIVWIDELDK
EDNVHCRMAE QEVGRRQGLL QPEVQWHGDG IVCMTMFLPA AERVAEFAAK SIGERMGFED
VEVIHKQIMH PAEGTLVEVK GRIPFAINPA ELVIPPVAET LTEDAIRQYV VDHKFKIVAA
TVGEDEHSVG LREILDIKHG GIERFGIECH YLGTSVPVEK LADAAIELGA DAVLASTVIS
HADIHRLNMR RLHQYCQERG IRDKLIVVCG GTQVTNELAV AEGMDAGFGR GTKGVHVASL
LVKRHKELGS DNNEHV
//
