KAME_FUSNN
ID KAME_FUSNN Reviewed; 263 AA.
AC Q8RHX8;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Lysine 5,6-aminomutase beta subunit {ECO:0000305};
DE Short=5,6-LAM {ECO:0000305};
DE EC=5.4.3.3 {ECO:0000250|UniProtKB:E3PRJ4, ECO:0000269|PubMed:6811551};
DE AltName: Full=D-lysine 5,6-aminomutase beta subunit {ECO:0000250|UniProtKB:E3PRJ4};
DE AltName: Full=L-beta-lysine 5,6-aminomutase beta subunit {ECO:0000312|EMBL:AAL93961.1};
GN OrderedLocusNames=FN1862;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355 {ECO:0000269|PubMed:6811551};
RX PubMed=6811551; DOI=10.1128/jb.152.1.201-207.1982;
RA Barker H.A., Kahn J.M., Hedrick L.;
RT "Pathway of lysine degradation in Fusobacterium nucleatum.";
RL J. Bacteriol. 152:201-207(1982).
RN [3]
RP IDENTIFICATION.
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355 {ECO:0000269|PubMed:17166837};
RX PubMed=17166837; DOI=10.1074/jbc.m609829200;
RA Kreimeyer A., Perret A., Lechaplais C., Vallenet D., Medigue C.,
RA Salanoubat M., Weissenbach J.;
RT "Identification of the last unknown genes in the fermentation pathway of
RT lysine.";
RL J. Biol. Chem. 282:7191-7197(2007).
CC -!- FUNCTION: Catalyzes the migration of the L-beta-lysine and D-lysine
CC epsilon amino group to the delta carbon to produce 3,5-diaminohexanoate
CC and 2,5-diaminohexanoate, respectively. {ECO:0000250|UniProtKB:E3PRJ4,
CC ECO:0000269|PubMed:6811551}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate;
CC Xref=Rhea:RHEA:21736, ChEBI:CHEBI:57434, ChEBI:CHEBI:57436;
CC EC=5.4.3.3; Evidence={ECO:0000269|PubMed:6811551};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-lysine = (2R,5S)-2,5-diaminohexanoate; Xref=Rhea:RHEA:18241,
CC ChEBI:CHEBI:32557, ChEBI:CHEBI:137487; EC=5.4.3.3;
CC Evidence={ECO:0000250|UniProtKB:E3PRJ4};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000250|UniProtKB:E3PRJ4};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:E3PRJ4};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via acetate
CC pathway. {ECO:0000269|PubMed:6811551}.
CC -!- SUBUNIT: Heterotetramer of 2 alpha and 2 beta subunits.
CC {ECO:0000250|UniProtKB:E3PRJ4}.
CC -!- SIMILARITY: Belongs to the KamE family. {ECO:0000255}.
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DR EMBL; AE009951; AAL93961.1; -; Genomic_DNA.
DR RefSeq; NP_602662.1; NC_003454.1.
DR AlphaFoldDB; Q8RHX8; -.
DR SMR; Q8RHX8; -.
DR STRING; 190304.FN1862; -.
DR EnsemblBacteria; AAL93961; AAL93961; FN1862.
DR KEGG; fnu:FN1862; -.
DR PATRIC; fig|190304.8.peg.338; -.
DR eggNOG; COG5012; Bacteria.
DR HOGENOM; CLU_065773_0_0_0; -.
DR InParanoid; Q8RHX8; -.
DR OMA; AIMNMKG; -.
DR BioCyc; FNUC190304:G1FZS-359-MON; -.
DR BioCyc; MetaCyc:MON-12293; -.
DR BRENDA; 5.4.3.3; 2370.
DR UniPathway; UPA00870; -.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0047702; F:beta-lysine 5,6-aminomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0047826; F:D-lysine 5,6-aminomutase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0019475; P:L-lysine catabolic process to acetate; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.30.60; -; 1.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR028991; KamE_N.
DR InterPro; IPR036843; KamE_N_sf.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF16554; OAM_dimer; 1.
DR SUPFAM; SSF117778; SSF117778; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 1: Evidence at protein level;
KW Cobalamin; Cobalt; Isomerase; Metal-binding; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..263
FT /note="Lysine 5,6-aminomutase beta subunit"
FT /id="PRO_0000416985"
FT DOMAIN 120..259
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT BINDING 130..136
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000250|UniProtKB:E3PRJ4"
FT BINDING 133
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /ligand_part="Co"
FT /ligand_part_id="ChEBI:CHEBI:27638"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:E3PRJ4"
FT BINDING 185..192
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000250|UniProtKB:E3PRJ4"
FT BINDING 219..223
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000250|UniProtKB:E3PRJ4"
FT BINDING 239..244
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000250|UniProtKB:E3PRJ4"
FT MOD_RES 144
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:E3PRJ4"
SQ SEQUENCE 263 AA; 28990 MW; C98859FD23A14FFF CRC64;
MSSGLYSTEK RDFDTTLDLT QIRPYGDTMN DGKVQMSFTL PVACNEKGIE AALQLARKMG
FVNPAVAFSE ALDKEFSFYV VYGATSFSVD YTAIKVQALE IDTMDMHECE KYIEENFGRE
VVMVGASTGT DAHTVGIDAI MNMKGYAGHY GLERYKGVRA YNLGSQVPNE EFIKKAIELK
ADALLVSQTV TQKDVHIENL TNLVELLEAE GLRDKIILIA GGARITNDLA KELGYDAGFG
PGKYADDVAT FILKEMVQRG MNK
