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KAL_FUSNN
ID   KAL_FUSNN               Reviewed;         128 AA.
AC   Q8RHX1;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=3-aminobutyryl-CoA ammonia lyase {ECO:0000303|PubMed:17166837};
DE            EC=4.3.1.14 {ECO:0000269|PubMed:17166837, ECO:0000269|PubMed:6811551};
DE   AltName: Full=3-aminobutyryl-CoA deaminase {ECO:0000303|PubMed:17166837};
GN   Name=kal {ECO:0000303|PubMed:17166837}; OrderedLocusNames=FN1869;
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;
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   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC   2640 / LMG 13131 / VPI 4355;
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: Involved in the anaerobic fermentation of lysine. Catalyzes
CC       the deamination of L-3-aminobutyryl-CoA to produce crotonoyl-CoA.
CC       {ECO:0000269|PubMed:17166837, ECO:0000269|PubMed:6811551}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-3-aminobutanoyl-CoA = (2E)-butenoyl-CoA + NH4(+);
CC         Xref=Rhea:RHEA:10056, ChEBI:CHEBI:28938, ChEBI:CHEBI:57332,
CC         ChEBI:CHEBI:57366; EC=4.3.1.14;
CC         Evidence={ECO:0000269|PubMed:17166837, ECO:0000269|PubMed:6811551};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=55.2 uM for crotonyl-CoA {ECO:0000269|PubMed:17166837};
CC         Vmax=150.9 nmol/min/ug enzyme with crotonyl-CoA as substrate
CC         {ECO:0000269|PubMed:17166837};
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via acetate
CC       pathway. {ECO:0000269|PubMed:6811551, ECO:0000305|PubMed:17166837}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:17166837}.
CC   -!- SIMILARITY: Belongs to the KAL family. {ECO:0000305}.
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DR   EMBL; AE009951; AAL93968.1; -; Genomic_DNA.
DR   RefSeq; NP_602669.1; NC_003454.1.
DR   AlphaFoldDB; Q8RHX1; -.
DR   SMR; Q8RHX1; -.
DR   STRING; 190304.FN1869; -.
DR   EnsemblBacteria; AAL93968; AAL93968; FN1869.
DR   KEGG; fnu:FN1869; -.
DR   PATRIC; fig|190304.8.peg.345; -.
DR   eggNOG; COG1607; Bacteria.
DR   HOGENOM; CLU_149200_0_0_0; -.
DR   OMA; YAGDYIE; -.
DR   BioCyc; FNUC190304:G1FZS-366-MON; -.
DR   BioCyc; MetaCyc:MON-12295; -.
DR   UniPathway; UPA00870; -.
DR   Proteomes; UP000002521; Chromosome.
DR   GO; GO:0047459; F:3-aminobutyryl-CoA ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019475; P:L-lysine catabolic process to acetate; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR033120; HOTDOG_ACOT.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR006683; Thioestr_dom.
DR   Pfam; PF03061; 4HBT; 1.
DR   SUPFAM; SSF54637; SSF54637; 1.
DR   PROSITE; PS51770; HOTDOG_ACOT; 1.
PE   1: Evidence at protein level;
KW   Lyase; Reference proteome.
FT   CHAIN           1..128
FT                   /note="3-aminobutyryl-CoA ammonia lyase"
FT                   /id="PRO_0000416979"
FT   DOMAIN          1..123
FT                   /note="HotDog ACOT-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
SQ   SEQUENCE   128 AA;  13960 MW;  D5AE3CF23CEE8F85 CRC64;
     MKSLIRLRMS SHDAHYGGNL VDGARMLQLF GDVATELLIQ LDGDEGLFKA YDSVEFMAPV
     FAGDYIEAEG EIVNVGNSSR KMVFEARKVI VPRPDISDSA ADVLAEPIVV CRATGTCVTP
     KDKQRGKK
 
 
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