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

1 structures for Q9KDS9

Entry ID Method Resolution Chain Position Source
AF-Q9KDS9-F1 Predicted AlphaFoldDB

No variants for Q9KDS9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9KDS9

No associated diseases with Q9KDS9

5 regional properties for Q9KDS9

Type Name Position InterPro Accession
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 116 - 322 IPR005479
domain Biotin carboxylase-like, N-terminal domain 1 - 110 IPR005481
domain Biotin carboxylase, C-terminal 336 - 441 IPR005482
domain ATP-grasp fold 120 - 317 IPR011761
domain Biotin carboxylation domain 1 - 445 IPR011764

Functions

Description
EC Number 6.3.4.14 Other carbon--nitrogen ligases
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

4 GO annotations of molecular function

Name Definition
acetyl-CoA carboxylase activity Catalysis of the reaction: ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
biotin carboxylase activity Catalysis of the reaction: ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein.
metal ion binding Binding to a metal ion.

2 GO annotations of biological process

Name Definition
fatty acid biosynthetic process The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
malonyl-CoA biosynthetic process The chemical reactions and pathways resulting in the formation of malonyl-CoA, the S-malonyl derivative of coenzyme A.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MFKKVLIANR GEIAVRIIRT CQKLNIRTVA IYSEADVDSL HVKHADEAFL IGKPPVAESY
70 80 90 100 110 120
LKVDTILEVA KQAGVDAIHP GYGLLSENAR FARACVEAGI SFIGPSPEVI ERMGSKIAAR
130 140 150 160 170 180
TAMQTAGVPV IPGSDVALAD EEEAVHLARK FGYPVMLKAS AGGGGIGMQL VRNDEEMRKA
190 200 210 220 230 240
FAGNQKRATS FFGDGTMFLE KAVENPRHIE VQIAADHHGH VVHLWERDCS IQRRHQKVVE
250 260 270 280 290 300
EAPSPFVDEA LREKIGQLAV KAAKAIDYRN LGTVECLVDG EKNIYFLEMN TRLQVEHPVT
310 320 330 340 350 360
EEITGIDLVE WQLLIAAGEQ LPYAQHEIPL QGHAIEVRIY AEDPVTFFPS PGMIKRFTLP
370 380 390 400 410 420
EGEGIRHEYA ISEGYKVTPF YDPMVAKLIV SADTRGEAIQ RLGRALKQYE IEGIKTNIPM
430 440 450
LKQVINHPVF QAGEATTAFV TNHLKVKTGR NP