ID A0A136JQ17_9BACT Unreviewed; 936 AA.
AC A0A136JQ17;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Long-chain fattyacid-CoA ligase {ECO:0000313|EMBL:KXJ99239.1};
GN ORFNames=UZ03_NOB001003236 {ECO:0000313|EMBL:KXJ99239.1};
OS Nitrospira sp. OLB3.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1617410 {ECO:0000313|EMBL:KXJ99239.1, ECO:0000313|Proteomes:UP000070691};
RN [1] {ECO:0000313|EMBL:KXJ99239.1, ECO:0000313|Proteomes:UP000070691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB3 {ECO:0000313|EMBL:KXJ99239.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Improved understanding of the partial-nitritation anammox process through
RT 23 genomes representing the majority of the microbial community.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KXJ99239.1}.
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DR EMBL; JZQY01000064; KXJ99239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136JQ17; -.
DR STRING; 1617410.UZ03_NOB001003236; -.
DR PATRIC; fig|1617410.3.peg.3318; -.
DR Proteomes; UP000070691; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000313|EMBL:KXJ99239.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840}.
FT DOMAIN 583..663
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 147..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 936 AA; 103234 MW; 7006A7BEF93A9446 CRC64;
MEHDAMPQER MRSHHREAVT LIELIQGLGS YGGQQALVAF HKQSVEVLTY HRLLQEADQL
TAVLIESGLQ KGERVLLYAP NSPAWIIAFL ALLRGAAVPV PIDSQMPSDD LAHVIRDSEA
RRLLTTHTLA KHVMALGHTQ HLATLFLDGD EGDPQNRQRS PRSGPPAIPT AQPDDHALLF
YTSGSSGRPK GVPLSHRNLL ANLNALVNER VYRADERLLL PLPLHHVYPF MVGLLAPLAQ
GLTIVLPHSL TGPHLRRALR EGRVTALVAV PRLLSALFQA IEQPFRERGS IAAALFHLML
RGSVTLLRWT GIRIGSHIFS PLHRRFAPHL STLVSGGSPL DPALSWNLAG LGWQIASGYG
LTETSPILTF FGPGRRQFDS AGRPLPGVDL RIADHDPETN QGEIQARGPN VFAGYLHLPD
KTREAFTADG WFRTGDLGFL DQQGRLHIVG RASSRITLPG GEKVWPESIE ERMDQGSAVA
ESAILLYGGR LVAIVVPRKK ALSMDQADEM RKAIRADLDT ALRDFPSYAR LTECVVSVDP
LPRTRLGKIQ RHKLAARFEE ASRADETDGL RRAPIAVDQM TPDDRQLLED PIVARTWDLL
TRRFPDRRLT PDSNLQLDLG LDSMDWMALT LDLHDRIGID LSLDRIARIG IVRDLLREAA
EATEAADAGV DPVEQLQHPD QLLSPWQRSW LAPRGWCFRT LGQLLHRIDR LLMRVLFQLE
VQGLEHLPPQ GPCVLAPNHV SLLDPPTLFA ALPPERLQRT SWGGWTGFMF RNLPMRLVSR
ATRILPIAQS TAALTDLALA GAALRRGDTL VWYAEGGLSR NGRLQPFQPG IGLLLTAYPV
PVLPVFVEGS FKALPPDSRR VHPRRLTIRF GASLSPDLLD GPPQGPERYR HIAAALHDRV
AALSDGTPVL PVVSLRENGY SATQIDGTGG NKEGNP
//
