ID A0A0S2I4Z9_9BACT Unreviewed; 360 AA.
AC A0A0S2I4Z9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=[Citrate [pro-3S]-lyase] ligase {ECO:0000256|PIRNR:PIRNR005751};
DE EC=6.2.1.22 {ECO:0000256|PIRNR:PIRNR005751};
GN Name=citC {ECO:0000313|EMBL:ALO17475.1};
GN ORFNames=L21SP5_03883 {ECO:0000313|EMBL:ALO17475.1};
OS Salinivirga cyanobacteriivorans.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC Salinivirga.
OX NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO17475.1, ECO:0000313|Proteomes:UP000064893};
RN [1] {ECO:0000313|EMBL:ALO17475.1, ECO:0000313|Proteomes:UP000064893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO17475.1,
RC ECO:0000313|Proteomes:UP000064893};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Description and complete genome sequence of a novel strain predominating
RT in hypersaline microbial mats and representing a new family of the
RT Bacteriodetes phylum.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-
CC dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
CC {ECO:0000256|PIRNR:PIRNR005751}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + holo-[citrate lyase ACP] = acetyl-[citrate
CC lyase ACP] + AMP + diphosphate; Xref=Rhea:RHEA:23788, Rhea:RHEA-
CC COMP:10158, Rhea:RHEA-COMP:13710, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:82683,
CC ChEBI:CHEBI:137976, ChEBI:CHEBI:456215; EC=6.2.1.22;
CC Evidence={ECO:0000256|PIRNR:PIRNR005751};
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DR EMBL; CP013118; ALO17475.1; -; Genomic_DNA.
DR RefSeq; WP_057954736.1; NZ_CP013118.1.
DR AlphaFoldDB; A0A0S2I4Z9; -.
DR STRING; 1307839.L21SP5_03883; -.
DR KEGG; blq:L21SP5_03883; -.
DR PATRIC; fig|1307839.3.peg.4144; -.
DR OrthoDB; 9779753at2; -.
DR Proteomes; UP000064893; Chromosome.
DR GO; GO:0008771; F:[citrate (pro-3S)-lyase] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR005216; Citrate_lyase_ligase.
DR InterPro; IPR013166; Citrate_lyase_ligase_C.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00124; cit_ly_ligase; 1.
DR PANTHER; PTHR40599; [CITRATE [PRO-3S]-LYASE] LIGASE; 1.
DR PANTHER; PTHR40599:SF1; [CITRATE [PRO-3S]-LYASE] LIGASE; 1.
DR Pfam; PF08218; Citrate_ly_lig; 1.
DR PIRSF; PIRSF005751; Acet_citr_lig; 1.
DR SMART; SM00764; Citrate_ly_lig; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR005751};
KW Ligase {ECO:0000256|PIRNR:PIRNR005751, ECO:0000313|EMBL:ALO17475.1};
KW Lyase {ECO:0000313|EMBL:ALO17475.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR005751};
KW Reference proteome {ECO:0000313|Proteomes:UP000064893}.
FT DOMAIN 1..138
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 360 AA; 41237 MW; 5AAF5724CCC1153C CRC64;
MSFENADFRE EVLDIENPFD VKFVSKFLKK LDFDYTPEDV DYTMVLYTLN DEIIGTGSYQ
NHVLKYVAVA PDYRSSAAFS QIVTHLMDKL LTRYKNIFVY TLPRNTKVFE GLGFTEIATA
PPLFSVLEFG YENIKTYQQY LRKQKQDVST GPVSAIVVNC NPFTNGHKYL IEKAAQESRI
LYLFVVEEDR SSFPFEVRWE LIKKGIAHLQ NVFMLKGGDY VVSGTIFPSY FLKNENPGMI
AEKQAELDIR TFIKYIVPVL GITRRYVGTE NYDATTLAYN NAMKTLLPRA GVKLIEINRK
KAATTTGETS VISASKVRQA IKDDRLSEIE EFLPESTRNY LKSNESAWIK AKIKSSNTRH
//
