ID A0A0D6KB35_9CYAN Unreviewed; 1453 AA.
AC A0A0D6KB35;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=AMP-binding enzyme {ECO:0000313|EMBL:EKE96607.1};
GN ORFNames=FDUTEX481_06512 {ECO:0000313|EMBL:EKE96607.1};
OS Tolypothrix sp. PCC 7601.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1188 {ECO:0000313|EMBL:EKE96607.1, ECO:0000313|Proteomes:UP000032761};
RN [1] {ECO:0000313|EMBL:EKE96607.1, ECO:0000313|Proteomes:UP000032761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX PubMed=25953173;
RA Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA Kehoe D.M., Weinstock G.M.;
RT "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT PCC 7601.";
RL Genome Announc. 3:0-0(2015).
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:EKE96607.1}.
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DR EMBL; AGCR01000135; EKE96607.1; -; Genomic_DNA.
DR STRING; 1188.FDUTEX481_06512; -.
DR PATRIC; fig|1188.3.peg.9917; -.
DR HOGENOM; CLU_000022_2_17_3; -.
DR Proteomes; UP000032761; Unassembled WGS sequence.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd12115; A_NRPS_Sfm_like; 1.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05235; SDR_e1; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR013120; Far_NAD-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR010080; Thioester_reductase-like_dom.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR NCBIfam; TIGR01746; Thioester-redct; 1.
DR PANTHER; PTHR44845:SF6; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PIRSF; PIRSF001617; Alpha-AR; 3.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 942..1017
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1453 AA; 164884 MW; D665BF304601404A CRC64;
MEKSMLSDHK NISIHQLVEF QVSRTPDAVA VIFQNEQLTY RELNQKANQL AHHLRTLGVK
PETLVGVCIE RSLEMVVALL GILKAGGAYI PLDPTYPKDR LAFIIEDTQI PILLTQEHLQ
ALVSQHQGYT VYINSDWQNI AQQPIDNPIS EVRPNNLAYV IYTSGSTGIP KGVAIEHRNT
IALIDWATEF FTPEQLKGVL ASTSICFDLS VFELFVTLCC GGRVILAQNA LELPNLPAAL
EVTLINTVPS AIAALLRMEG IPSSVKTINL AGEPLQNALV QQLYQLEHIQ QVFNLYGPTE
DTTYSTVALI RKGSTEIPSI GRPLPNTKIY LLEVPSRRKN DRLKPVPMGV AGELYISGSG
LARGYLNRPD LTSEKFILHS LNQETEVRLY RTGDLAVYLP DGNLKFLGRI DHQIKIRGFR
VELGEVEAAI NQYPGIRESV VIPRDGEFGD KRLVAYIVPK THNDLEQLKP MDQLYTKQLQ
EWRNVWDATY SQPYEDVDPT FNFISWNDSF TGLPIPVDEM HEYVNSTVKH ILSLKPQRVL
EIGCGNGLLL FRIAPHCSHY FGTDISKQAI HYIEQQLNKS KPNWSHVKVS EGAAHELEGL
EVGSFDTVII NSVIQYFPSV DYFLQVIEKV VRLLKPGGQI FIGDVRSLPL LETFHTAVQL
SQAIASLSSN QLQKIVRERM LHERELVLHP TFFSTLKQRI PRINHVQTFL KRGQSQNELI
RFRFDVILHV EADTYQDLEP LCWDWQQQEL SIPLICKFLQ EQQPKILKII NVPNARVFLD
VKAVELLASN SKATTVGQLR ETLWQIHEYT RVHPEEFWNI SQDLPYNAHI TWSELNAPGT
YDVVLQSQLK IIEQKAIPIL PEQPLKLKPL SAYANNPLQV NEKSKLGLKL RTYLKEKLPH
YMVPSAFVVM ETLPLTTNGK IDRRSLPEPK KERPMLKEAY IAPSNLIEQQ LAEIWSQILG
IEQVGIYDNF FELGGHSLVT AHLLSQVEEV THVKVSLSYF LREPTIAGLI KAINTNQNLD
CDVNFGAENQ IDLYTEAILD PTIYPELPFV ESKNEPKHIF LTGVTGFLGA FLLDELLKQT
PANIYCLVRA SNIEHGRQKI QTNLERYKLG NSKLSSKVIP ILGDLSQPLL GLTSANFREL
GNKLDLIYHA GALVNLVYPY NTLRATNVLG TQEILRLASQ GKATPVHFIS TIDVLKPLIF
RGKKTITEDE QLDNPYELKQ GYTQTKWVAE KLVIAAQSRG IPTCIYRPGM MSGHSQTGVS
QTNDLINRII KGMIQMGSAP TWEQWINLTP IDYASKAILY LSRQRKSLGK VFHIVNPNPL
FWNDIVTNIQ NFGYYIRILP YDKWQAELLK LDIEQENALE PIIPLFTENI FNNQMTYLEI
FLRTSTVFDC RKTLDMLVDT SIICPTINAN MLQSYFDYLI NKSFIKLPKY EIDKSFDKDI
IKTISECENM AKN
//
