Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

3 structures for P19913

Entry ID Method Resolution Chain Position Source
1FFU X-ray 235 A B/E 1-803 PDB
1FFV X-ray 225 A B/E 1-803 PDB
AF-P19913-F1 Predicted AlphaFoldDB

No variants for P19913

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P19913

No associated diseases with P19913

3 regional properties for P19913

Type Name Position InterPro Accession
domain Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead 32 - 141 IPR000674
domain Aldehyde oxidase/xanthine dehydrogenase, first molybdopterin binding domain 173 - 419 IPR008274
domain Aldehyde oxidase/xanthine dehydrogenase, second molybdopterin binding domain 447 - 734 IPR046867

Functions

Description
EC Number 1.2.5.3 With a quinone or similar compound as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

5 GO annotations of molecular function

Name Definition
carbon-monoxide dehydrogenase (acceptor) activity Catalysis of the reaction: CO + H2O + acceptor = CO2 + reduced acceptor.
carbon-monoxide oxygenase activity Catalysis of the reaction: CO + H2O + ferrocytochrome b-561 = CO2 + 2 H+ + 2 ferricytochrome b-561.
copper ion binding Binding to a copper (Cu) ion.
iron ion binding Binding to an iron (Fe) ion.
molybdenum ion binding Binding to a molybdenum ion (Mo).

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNAPVQDAEA RELALAGMRP RACAKEDARF IQGKGNYVDD IKMPGMLHMD IVRAPIAHGR
70 80 90 100 110 120
IKKIHKDAAL AMPGVHAVLT AEDLKPLKLH WMPTLAGDVA AVLADEKVHF QMQEVAIVIA
130 140 150 160 170 180
DDRYIAADAV EAVKVEYDEL PVVIDPIDAL KPDAPVLRED LAGKTSGAHG PREHHNHIFT
190 200 210 220 230 240
WGAGDKAATD AVFANAPVTV SQHMYYPRVH PCPLETCGCV ASFDPIKGDL TTYITSQAPH
250 260 270 280 290 300
VVRTVVSMLS GIPESKVRIV SPDIGGGFGN KVGIYPGYVC AIVASIVLGR PVKWVEDRVE
310 320 330 340 350 360
NISTTAFARD YHMDGELAAT PDGKILGLRV NVVADHGAFD ACADPTKFPA GLFHICSGSY
370 380 390 400 410 420
DIPRAHCSVK GVYTNKAPGG VAYRCSFRVT EAVYLIERMV DVLAQKLNMD KAEIRAKNFI
430 440 450 460 470 480
RKEQFPYTTQ FGFEYDSGDY HTALKKVLDA VDYPAWRAEQ AARRADPNSP TLMGIGLVTF
490 500 510 520 530 540
TEVVGAGPSK MCDILGVGMF DSCEIRIHPT GSAIARMGTI TQGQGHQTTY AQIIATELGI
550 560 570 580 590 600
PSEVIQVEEG DTSTAPYGLG TYGSRSTPVA GAAIALAARK IHAKARKIAA HMLEVNENDL
610 620 630 640 650 660
DWEVDRFKVK GDDSKFKTMA DIAWQAYHQP PAGLEPGLEA VHYYDPPNFT YPFGIYLCVV
670 680 690 700 710 720
DIDRATGETK VRRFYALDDC GTRINPMIIE GQIHGGLTEG YAVAMGQQMP FDAQGNLLGN
730 740 750 760 770 780
TLMDYFLPTA VETPHWETDH TVTPSPHHPI GAKGVAESPH VGSIPTFTAA VVDAFAHVGV
790 800
THLDMPHTSY RVWKSLKEHN LAL