ID   A0A1Q7WB27_9ACTN        Unreviewed;       538 AA.
AC   A0A1Q7WB27;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=ATP-citrate synthase/succinyl-CoA ligase C-terminal domain-containing protein {ECO:0000259|Pfam:PF00549};
GN   ORFNames=AUG49_03870 {ECO:0000313|EMBL:OLE27934.1};
OS   Catenulispora sp. 13_1_20CM_3_70_7.
OC   Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC   Catenulisporaceae; Catenulispora.
OX   NCBI_TaxID=1805055 {ECO:0000313|EMBL:OLE27934.1, ECO:0000313|Proteomes:UP000186605};
RN   [1] {ECO:0000313|EMBL:OLE27934.1, ECO:0000313|Proteomes:UP000186605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
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:OLE27934.1}.
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DR   EMBL; MNJN01000063; OLE27934.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7WB27; -.
DR   Proteomes; UP000186605; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR   InterPro; IPR005811; SUCC_ACL_C.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR11117:SF2; SUCCINATE--COA LIGASE [ADP_GDP-FORMING] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11117; SUCCINYL-COA LIGASE SUBUNIT ALPHA; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
PE   4: Predicted;
FT   DOMAIN          362..526
FT                   /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00549"
FT   REGION          70..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   538 AA;  55730 MW;  1CC33018E7D4428B CRC64;
     MLAARAVAGV AGVERVLVAM GTELNIELLT ALGYPPPRPT AGPADLMIAF TCPDEATEAT
     ALTTLTASLT PGGPITASGH QPPDRPLPRT TGSALGRTSA PLTLISTPGL ASVPEAMESL
     QHGASVVIFS DNIPIHHEIR LKEEARRRSL LVMGPDCGTV VLQGIGLGFA NATRPGPISL
     VAASGTGAQQ LMSLLDAAGT GIRHCLGVGG RDLTEPVAGR STHAALDILA EDEETTLIVL
     ISKPPHPAVA RSIEEHASRL PKPVILAFIG PDQPTLTTTT ERILATLHHT PTPTWPHWAP
     SADDDARAVS DGSGQAARES DPGRAAAPDA DPGRPPRTAD SDRTGPGQAA QEADPSRTIR
     GLFSGGTLCA EAEVVLTRVL AEQLGGWGEG ESRKLKKTTP QAPPEPHAPF TPHLTDFGDD
     TYTRGRPHPM IDNTLRLRAI AEAAADPRVG VLLLDVVLGR GAHPDPAGEL VPAVVAARAE
     RRLPVVVSLC GTAGDPQGLE RQARAFADAG AWVYLSNAEA ATAAARLVPR RPSGGGDE
//